Download Central Dogma of Molecular Biology: The way of diverting

International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
Central Dogma of Molecular Biology: The way of diverting the instruction from DNA to
protein synthesis and this change ultimately make the conversion of organism
into another organism
Priyank Bharati*1, Garima Tyagi2
P
P
P
*1 Assistant Professor, School of Biological Engineering, Shobhit University, Adarsh
Instutuional Area, Babu Vijendra Marg, Gangoh, Distt. Saharanpur - 247341. U.P., India
0T
0T16
16T
2 Natural Sciences Trust, Meerut, U.P., India
Abstract
“MayaviShaktiya”, “Chamatkar” these things are beyond any religious belief but which used
to happen and will continue to happen even in future if a person will have deep knowledge as
well as better understanding of scientific concept behind it. This is again an example of the
developed Vedic Sciences which is still unreachable by current people. It is also clear that
there was not any laboratory apparatus as used these days and people used to synthesize
natural chemicals in place of artificial chemicals that time for their work even if we talk of
the Birth of Kauravas in Mahabharata or to commute the physical morphology in Ramayana.
Our daily life also has science in it, that depends on our observation and perception that how
we co-relate both. In this research paper we are explaining about the methodology to
commute the physical morphology which is a scientific process controlled by central dogma
of molecular biology which shows that DNA forms the RNA which finally forms proteins
and these proteins determines the structural and functional properties of a body.
Keywords: - Central Dogma, Proteins, Amino Acids
Introduction
deer which shows that this technique was
All of us have heard somewhere or even
also known by people at that time. In
seen in the television that a person changes
Mahabharata also Shri Krishna was
his the entire body and takes up the
expert in this technique and at the time of
morphology of some different species like
Kurukshetra War, he showed his enlarged
“Ichadhari
Some
body size (vikraal roop) which explains
evidences like this are also mentioned in
that his bones were flexibility (due to
Ramayana, that at the time of Sita haran, a
contractile protein). We generally study
person took the morphology of golden
and link all these things to religion
naag
and
nagin”.
(dhrama) and give them a name of
324
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
“chamatkar or Mayavi shaktiya”. Even
enzymes are proteins. Around 300 amino
Science has always denied such things
acids occur in nature but 20 of them are
which are conceptually a part on science
found in proteins. These amino acids are
only. In this 21st century, researches are
known as “Standard or Principle amino
going on in various fields, in various parts
acids” .In proteins the amino acids are
of the World to know that which
linked up by polypeptide bonds to form
techniques were used at that time. If we
long chain called polypeptides. Proteins
are talking of such powers then we must
are like long necklaces with differently
first study the process responsible for all
shaped beads. Each "bead" is a small
this. This paper will explain the scientific
molecule called an amino acid. There are
concept behind these type of processes.
20 standard amino acids, each with its own
P
P
shape,
Proteins: Structural and Functional
size,
and
properties.
Proteins
typically contain from 50 to 2,000 amino
Unit
acids hooked end to end in many
Proteins are the most abundant molecule
combinations. Each protein has its own
within the living cells. Proteins are basic
sequence of amino acids [1]. Proteins are
and functional unit of life.. Scientific
primarily responsible for structure and
literatures show that proteins constitute
strength of body. Muscles contraction in
about 50% of the cellular dry weight. The
higher organism and flagella movement in
term protein is derived from a Greek word
micro-organism takes place by contractile
proteios meaning holding the first place.
assemblies. These contractile assemblies
Berzelius (Swedish chemist) suggested the
are made up of Proteins e.g. actin and
name proteins to the group of organic
myosin proteins play important role in
compounds that are utmost important to
muscles contraction.
life. Mulder (Dutch chemist) in 1838 used
generally assumed that genes were made
the term proteins for the high molecular
of protein, since proteins were the only
weight nitrogen- rich and most abundant
biochemical entities that, at the time,
substances present in animals and plants.
seemed complex enough to serve as agents
Protein contains 50-55% of Carbon, 6-7%
of inheritance.
Hydrogen,
15-18%
Proteins are worker molecules that are
Nitrogen and 0-4% Sulphur.. They are
necessary for virtually every activity in
widely distributed in living matter. All
your body [1]. Proteins carry out a diverse
19-24%
Oxygen.
325
Till 1940s, it was
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
array of functions, including catalysis,
transports oxygen in muscle. Iron
defense, transport of substances, motion
is transported in blood by the
and regulation of cell and body functions.
protein transferrin.
•
The proteins within living organisms are
immensely
and
proteins play structural roles; these
function They perform following functions
structural proteins include keratin
[2]
in hair, fibrin in blood clots, and
•
diverse
in
structure
Support. Fibrous, or threadlike,
Enzyme catalysis. One class of
collagen, which forms the matrix of
proteins,
are
skin, ligaments, tendons, and bones
biological catalysts that facilitate
and is the most abundant protein in
specific
a vertebrate body.
enzymes,
which
chemical
reactions.
•
Because of this property, the
•
appearance of enzymes was one of
the sliding motion of two kinds of
the most important events in the
protein filament: actin and myosin.
evolution of life. Enzymes are
Contractile proteins also play key
globular proteins, with a three
roles in the cell’s cytoskeleton and
dimensional shape that fits snugly
in moving materials within cells.
around the chemicals they work on,
By the use of this protein Shri
facilitating chemical reactions by
Krishna moulded his body in the
stressing particular chemical bonds.
war of Mahabharata and made
Defense. Other globular proteins
them flexible. Similar types of
use their shapes to “recognize”
properties were observed in the
foreign microbes and cancer cells.
body of “Karan” and “Draupadi”.
These cell surface receptors form
[3]
•
the core of the body’s hormone and
•
Motion. Muscles contract through
Regulation. Small proteins called
immune systems.
hormones serve as intercellular
Transport. A variety of globular
messengers in animals. Proteins
proteins transport specific small
also play many regulatory roles
molecules and ions. The transport
within the cell, turning on and
protein hemoglobin, for example,
shutting
transports oxygen in the blood, and
development,
myoglobin,
addition,
a
similar
protein,
326
off
genes
for
proteins
during
example.
also
In
receive
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
information, acting as cell surface
receptors.
Table 1: Function of Proteins [2]
Structure of Proteins [2]
that distinguish the various amino acids
The structure of proteins is discussed in
play no role in the peptide backbone of
terms of four levels of structure, as
proteins, a protein can consist of any
primary,
sequence of amino acids. Thus, a protein
secondary,
tertiary,
and
quaternary
containing 100 amino acids could form
Primary Structure-The specific amino
any
acid sequence of a protein is its primary
sequences (that’s the same as 10130, or 1
structure. This sequence is determined by
followed by 130 zeros—more than the
the nucleotide sequence of the gene that
number of atoms known in the universe).
of
20100
P
P
different
amino
P
encodes the protein. Because the R groups
327
acid
P
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
This is an important property of proteins
sometimes “super secondary structure.”
because it permits such great diversity.
One very common motifis the β α β motif,
Secondary Structure-The amino acid side
which creates a fold or crease; the so
groups are not the only portions of proteins
called “Rossmann fold” at the core of
that form hydrogen bonds. The —COOH
nucleotide binding sites in a wide variety
and —NH 2 groups of the main chain also
of proteins is a β α β α β motif. A second
form quite good hydrogen bonds—so good
motif that occurs in many proteins is the β
that their interactions with water might be
barrel, a β sheet folded around to form a
expected to offset the tendency of non-
tube. A third type of motif, the α turn α
polar side groups to be forced into the
motif, is important because many proteins
protein interior. Inspection of the protein
use it to bind the DNA double helix.
structures determined by X-ray diffraction
Tertiary Structure- The final folded
reveals why they don’t —the polar groups
shape of a globular protein, which
of the main chain form hydrogen bonds
positions the various motifs and folds non
with each other. Two patterns of H
polar side groups into the interior, is called
bonding occur. In one, hydrogen bonds
a protein’s tertiary structure. A protein is
form along a single chain, linking one
driven into its tertiary structure by
amino acid to another farther down the
hydrophobic interactions with water. The
chain. This tends to pull the chain into a
final folding of a protein is determined by
coil called an alpha (α) helix. In the other
its primary structure—by the chemical
pattern, hydrogen bonds occur across two
nature of its side groups. Many proteins
chains, linking the amino acids in one
can be fully unfolded (“denatured”) and
chain to those in the other. Often, many
will spontaneously refold back into their
parallel chains are linked, forming a
characteristic shape .The stability of a
pleated, sheet like structure called a β-
protein, once it has folded into its 3-D
pleated sheet. The folding of the amino
shape, is strongly influenced by how well
acid chain by hydrogen bonding into these
its interior fits together. When two non
characteristic coils and pleats is called a
polar chains in the interior are in very
protein’s secondary structure.
close proximity, they experience a form of
R
Motifs-
R
The
elements
of
secondary
molecular attraction called Van der Waal’s
structure can combine in proteins in
forces. Individually quite weak, these
characteristic ways called motifs, or
forces can add up to a strong attraction
328
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
when many of them come into play, like
experimentally by artificially producing
the combined strength of hundreds of
the fragment of polypeptide that forms the
hooks and loops on a strip of Velcro. They
domain in the intact protein, and showing
are effective forces only over short
that the fragment folds to form the same
distances, however; there are no “holes” or
structure as it does in the intact protein. A
cavities in the interior of proteins. That is
single polypeptide chain connects the
why there are so many different non polar
domains of a protein, like a rope tied into
amino acids (alanine, valine, leucine,
several adjacent knots. Often the domains
isoleucine). Each has a different sized R
of
group, allowing very precise fitting of non
functions—one domain of an enzyme
polar chains within the protein interior.
might bind a cofactor, for example, and
Now you can understand why a mutation
another the enzyme’s substrate.
that converts one non polar amino acid
Quaternary Structure- When two or
within the protein interior (alanine) into
more polypeptide chains associate to form
another (leucine) very often disrupts the
a functional protein, the individual chains
protein’s stability; leucine is a lot bigger
are referred to as subunits of the protein.
than alanine and disrupts the precise way
The subunits need not be the same.
the chains fit together within the protein
Hemoglobin, for example, is a protein
interior. A change in even a single amino
composed of two α-chain subunits and two
acid can have profound effects on protein
β-chain subunits. A protein’s subunit
shape and can result in loss or altered
arrangement
function of the protein.
structure.
Domains-Many proteins in our body are
subunits, the interfaces where the subunits
encoded within our genes in functional
contact one another are often non polar,
sections called exons. Each exon-encoded
and play a key role in transmitting
section of a protein, typically 100 to 200
information between the subunits about
amino acids long, folds into a structurally
individual subunit activities. A change in
independent functional unit
a
the identity of one of these amino acids
domain. As the polypeptide chain folds,
can have profound effects. Sickle cell
the domains fold into their proper shape,
hemoglobin is a mutation that alters the
each more-or-less independent of the
identity of a single amino acid at the
others.
corner of the β subunit from polar
This
can
be
called
demonstrated
329
a
protein
In
is
have
called
proteins
quite
its
separate
quaternary
composed
of
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
glutamate to non polar valine putting a non
information
polar amino acid on the surface creates a“
organism is can be copied and passed
sticky patch” that causes one hemoglobin
down to its descendants. For this reason,
molecule to stick to another, forming long
DNA is often referred to as the hereditary
non functional chains and leading to the
material. Cells use the alternative form of
cell
nucleic acid, RNA, to read the cell’s DNA-
sickling
characteristic
of
this
that
specifies
what
an
hereditary disorder.
encoded
Central Dogma of Molecular Biology:
Scientific process which hold “Mayavi
Shaktiya”
synthesis of proteins. RNA is similar to
The biochemical activity of a cell depends
This transcript passes out into the rest of
on production of a large number of
the cell, where it serves as a blueprint
proteins, each with a specific sequence.
specifying
The ability to produce the correct proteins
sequence.
is
of
The central dogma states that once
protein
information has passed into proteins it
molecules themselves are not [2].Nucleic
cannot get out again in more detail, the
acids are the information storage devices
transfer of information from nucleic acid
of cells, just as disks or tapes store the
to protein may be possible, but transfer
information that computers use, blueprints
from protein to protein, or from protein to
store the information that builders use, and
nucleic
road maps store the information that
information
tourists use. There are two varieties of
determination of sequence, either of bases
nucleic
Acid
in the nucleic acid or of amino acid
(DNA) and Ribonucleic Acid (RNA). The
residues in protein [5]. The quotation
way
the
above is from a seminal paper, ‘On Protein
information used to assemble proteins is
Synthesis,’ presented by Francis Crick at
similar to the way in which the letters on a
the 1957 annual meeting of the Society of
page encode information. Unique among
Experimental Biology and published in
macromolecules, nucleic acids are able to
1958. In this paper, Crick listed the
serve as templates to produce precise
standard set of 20 amino acid residues for
copies
the first time; argued that ‘the specificity
passed
organisms,
between
even
acids:
in
which
of
generations
though
the
Deoxyribonucleic
DNA
themselves,
encodes
so
that
information
and
direct
the
DNA in structure and is made as a
transcripted copy of portions of the DNA.
the
330
a
acid
protein’s
is
means
amino
impossible.
the
acid
Here
precise
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
of a piece of nucleic acid is expressed
considered outside the dogma and “would
solely by the sequence of its bases, and
shake the whole intellectual basis of
that this sequence is a (simple) code for the
molecular biology.”[6] This DNA/nucleic
amino acid sequence of a particular
acid-centred view is still dominant in
protein’; argued that the 3-D conformation
virtually
of a protein must be determined by its
biological questions, ranging from the role
amino acid sequence; pointed out that
of heredity in disease to arguments about
protein synthesis must be sequential; and
the process of evolutionary change. Even
presented his hypothesis of ‘adaptor’
in the technical literature, there is a
molecules mediating protein formation at
widespread assumption that DNA, as the
the ribosome. Most importantly, Crick
genetic material, determines cell action
formulated what he called the ‘Central
and that observed deviations from strict
Dogma’ When the structure of DNA was
genetic determinism must be the result of
figured out in 1953, there was a strong
stochastic processes [7].
belief among the pioneers of the new
Protein Synthesis [8]
science of molecular biology that they had
all
public
discussions
of
The sequence of amino acids has a bearing
uncovered the physic chemical basis of
on the properties of a protein, and is
heredity and fundamental life processes
characteristic for a particular protein. The
[4]. Following discoveries about the
basic mechanism of protein synthesis is
process of protein synthesis, the consensus
that DNA makes RNA, which in turn
view was most cogently summarized a
makes protein. The central dogma of
half-century again 1958[5] (and then again
protein synthesis is expressed as follows:
in 1970[6]) by Crick’s declaration of “the
central dogma of molecular biology.” The
concept was that information basically
flows from DNA to RNA to protein,
which
determines
the
cellular
and
organismal phenotype. While it was
Fig 1 :- Process of Central Dogma
considered a theoretical possibility that
Proteins are widely used in cells to serve
RNA could transfer information into
diverse functions. Some proteins provide
DNA, information transfer from proteins
the structural support for cells while others
to DNA, RNA, or other proteins was
act
331
as
enzymes
to
catalyze
certain
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
reactions. We have already seen the roles
differs from DNA by the substitution of
that different enzymes play in building the
uracil (U) for thymine (T). Also, because
cell's structure and in catalyzing metabolic
only one strand of mRNA is needed when
reactions, but where do proteins come
synthesizing proteins, mRNA naturally
from?
exists in single-stranded forms.
Since the beginning of evolution, cells
have developed the ability to synthesize
proteins. They can produce new proteins
either for reproduction or to simply replace
a degraded one. To manufacture proteins,
cells follow a very systematic procedure
that first transcribes DNA into mRNA
(messenger RNA) and then translates the
mRNA into chains of amino acids. The
amino acid chain then folds into specific
proteins.
Protein synthesis mainly done in two
steps: transcription and translation.
TranscriptionU
Protein synthesis begins in the cell's
Fig 2: Eukaryotic cell show the place
nucleus when the gene encoding a protein
where translation and transcription
is copied into RNA (Fig 2). Genes, in the
takes place [9]
form of DNA, are embedded in in the cell's
After
chromosomes. The process of transferring
Transcription
helps
the
mRNA
is
transported out of the cell's nucleus
the gene's DNA into RNA is called
transcription.
transcription,
through nuclear pores to go to the site of
to
translation,
magnify the amount of DNA by creating
the
rough
endoplasmic
reticulum (Rough endoplasmic reticulum
many copies of RNA that can act as the
is named for its rough appearance, which
template for protein synthesis. The RNA
is due to the ribosomes attached to its
32T
copy of the gene is called the mRNA.
outer
DNA and RNA are both constructed by a
0T32
(cytoplasmic)
0T
surface.
Rough
Endoplasmic Reticulum lies immediately
chain of nucleotides. However, RNA
adjacent to the cell nucleus, and its
0T
332
0T32
32T
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
membrane is continuous with the outer
transcript. In the synthesis of proteins,
membrane of the nuclear envelope. The
there are actually three types of RNA that
ribosomes
participate and play different roles:
0T
0T32
on
32T
rough
0T
0T
Endoplasmic
Reticulum specialize in the synthesis of
a. mRNA(messenger RNA) carries the
proteins that possess a signal sequence that
genetic information from DNA and is used
directs
as a template for protein synthesis.
them
specifically
to
the
Endoplasmic Reticulum for processing. (A
b. rRNA(Ribosomal RNA)which is a
number of other proteins in a cell,
major constituent of the cellular particles
including
called
those
destined
for
ribosomes
on
which
protein
the nucleus and mitochondria, are targeted
synthesis actually takes place.
for synthesis on free ribosomes, or those
c. tRNA (transfer RNA) molecules, each
not attached to the Endoplasmic Reticulum
of which incorporates a particular amino
membrane). Proteins synthesized by the
acid subunit into the growing protein when
rough
it recognizes a specific group of three
0T
0T32
0T32
0T
0T
0T32
32T
Endoplasmic
Reticulum
have
specific final destinations. Some proteins,
adjacent bases in the mRNA.
for
the
DNA maintains genetic information in the
Endoplasmic Reticulum, whereas others
nucleus. RNA takes that information into
are sent to the Golgi apparatus, which lies
the cytoplasm, where the cell uses it to
next to the Endoplasmic Reticulum.
construct specific proteins, RNA synthesis
Proteins
is
example,
0T
remain
within
0T32
32T
secreted
from
the Golgi
0T
0T32
transcription;
protein
synthesis
is
apparatus are directed to lysosomes or to
translation. RNA differs from DNA in that
the cell membrane; still others are destined
it is single stranded, contains Uracil
for secretion to the cell exterior. Proteins
instead of Thymine and ribose instead of
targeted
Golgi
deoxyribose, and has different functions.
apparatus are transferred from ribosomes
The central dogma depicts RNA as a
on rough Endoplasmic Reticulum into the
messenger between gene and protein, but
rough Endoplasmic Reticulum lumen,
does not adequately describe RNA's other
which serves as the site of protein folding,
function.
modification, and assembly)[10].
Transcription is highly controlled and
Transcription is a process of making an
complex.
RNA strand from a DNA template, and the
expressed as required, and in multicellular
RNA molecule that is made is called
organisms, specialized cell types express
0T32
32T
0T
0T
0T32
for
0T32
0T32
0T
0T
transport
0T
to
the
0T32
0T32
0T
333
In
Prokaryotes,
genes
are
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
subsets of gene. Transcription factors
chain elongates, the large ribosomal
recognize sequences near a gene and bind
subunit attaches and the appropriate
sequentially,
binding
anticodon parts of tRNA molecules form
transcription. Transcription proceeds as
peptide bonds, a polypeptide grows. At a
RNAP inserts complementary RNA bases
stop codon, protein synthesis ceases.
opposite the coding strand of DNA.
Protein folding begins as translation
Antisense RNA blocks gene expression.
proceeds, with enzymes and chaperone
Messenger RNA transmits information in a
proteins assisting the amino acid chain in
gene to cellular structures that build
assuming
proteins. Each three mRNA bases in a row
Translation is efficient and economical, as
forms a codon that specifies a particular
RNA, ribosomes, enzymes, and key
amino acid. Ribosomal RNA and proteins
proteins are recycled.
form ribosomes, which physically support
RNA
the other participants in protein synthesis
following components
and help catalyze formation of bonds
The enzyme RNA polymerase
creating
a
its
final
functional
transcription
form.
requires
the
betweens amino acids.
 A DNA template
In eukaryotes, RNA is often altered before
 All four types of ribonucleoside
it is active. Messenger RNA gains a cap of
triphosphates (ATP, GTP and UTP)
++
modified nucleotides and a poly A tail.
++
 Divalent metal ions Mg or Mn as
P
P
Introns are transcribed and cut out, and
a co-factor
exons are reattached by ribozymes. RNA
 No primer is needed for RNA
editing introduced bases changes that alter
synthesis
the protein product in different cell types.
The
genetic
code
is
triplet,
P
P
 RNA transcription is a process that
non-
involves the following steps:
overlapping, continuous, universal, and
•
degenerate. As translation begins, mRNA,
Binding of RNA polymerase to
DNA Double Helix
tRNA with bound amino acids, ribosomes,
The histone coat protecting the DNA
energy molecules and protein factors
double helix of the gene to be transcribed
assemble. The mRNA leader sequence
is removed, on a signal from the
binds to rRNA in the small subunit of a
cytoplasm, exposing the polynucleotide
ribosome, and the first codon attracts a
sequences in this region of DNA. The
tRNA bearing methionine. Next, as the
RNA polymerase enzyme binds to a
334
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
specific site, called promoter, in the DNA
uridine monophosphate (UMP) as a result
double helix. This site is located on the 5
of their combining with ATP. The enzyme
side of the gene to be transcribed. It
phosphorylase catalyses this activation
signals the beginning of RNA synthesis.
process. The ribonucleotide triphosphates
The promoter also determines the DNA
are joined to the bases of the DNA
strand that is to be transcribed.
template chain one by one by hydrogen
•
bonding according to the base pairing rule
Exposure of RNA Bases
The histone coat protecting the DNA
i.e., A U, U A, C G, G C. This base pairing
double helix of the gene to be transcribed
is brought about by the RNA polymerase
is removed, on a signal from the
cytoplasm, exposing the polynucleotide
sequences in this region of DNA. The
RNA polymerase enzyme binds to a
specific site, called promoter, in the DNA
double helix. This site is located on the 5
side of the gene to be transcribed. It
signals the beginning of RNA synthesis.
Fig 3:- Synthesis of mRNA from DNA
The promoter also determines the DNA
[11]
strand that is to be transcription is not
• Conversion
Ribonucleoside
Monophosphates
known.
•
to
The various ribonucleoside triphosphates
Base pairing
The ribonucleoside triphosphates, namely,
on linking to the DNA template chain
adenosine triphosphate (ATP), guanosine
break off their high-energy bonds. This
triphosphate (GTP), cytidine triphosphate
changes
(CTP) and uridine triphosphate (UTP),
monophosphates
floating free in the nucleus, serve as the
normal components of RNA, and sets free
raw material for RNA synthesis. They are
pyrophosphate
formed by activation (phosphorylation) of
Pyrophosphate contains a high-energy
ribonucleoside
viz.,
bond (~). It undergoes hydrolysis by the
monophosphates,
them
to
which
ribonucleoside
represent
groups
the
(P~P).
adenosine
monophosphate
(AMP),
enzyme pyrophosphotase, releases energy
guanosine
monophosphate
(GMP),
and sets free inorganic phosphate Pi. The
cytidine
monophosphate
(CMP)
first ribonucleotide phosphate retains all
and
335
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
the
three
phosphates
chemically
distinct
and
from
is,
thus,
As the RNA chain grows, the transcribed
the
other
region of the DNA molecule gets hydrogen
nucleotides added after it.
•
Each
bonded to the opposite strand and the two
become spirally coiled to assume the
Formation of RNA Chain
ribonucleoside
original double helical form. When the last
monophosphate
attached to the DNA template chain then
ribonucleotide
combines with the ribonucleotide arrived
polymerase and RNA chain are completely
earlier, making the RNA chain become
released from the DNA, and now the DNA
longer. The process is catalysed by the
completes its winding into a double helix.
enzyme RNA polymerase and requires a
The protective protein coat is added again
divalent ion Mg++ or Mn ++. The RNA
to the DNA duplex.
chain, thus formed, contains nitrogenous
The sequence of nitrogen bases from the
bases that are complementary to those of
promoter to the terminator sites form a
the template DNA chain.
transcription unit. It may include one or
•
is
added,
the
RNA
more genes. An entire transcription unit
Separation of RNA Chain
As transcription proceeds, the hybrid
gets transcribed into a single RNA chain.
DNA-RNA molecule dissociates, partly
Processing of RNAs
releasing
under
The forms of RNAs originally transcribed
synthesis. When polymerase reaches a
from DNA are called primary transcripts.
terminator signal on the DNA, it leaves the
These undergo extensive changes, termed
DNA. The fully formed RNA chain is now
processing
totally released by this process; one gene
modification of RNAs, before they can
forms several molecules of RNA, which
become functional in both prokaryotes and
get released from the DNA template one
eukaryotes.
the
RNA
molecule
1.
after the other. In some cases, such as in E.
or
post-transcriptional
Larger RNA precursors are cut into
coli, a specific chain terminating protein,
smaller RNAs by a ribonuclease-P
called rho factor (P), stops the synthesis of
cleaving enzyme
RNA chain. In most cases, the enzyme
2.
RNA polymerase on its own can stop
by enzymes called nucleases (splicing)
transcription.
3.
•
Return
of
DNA
Segment
Unwanted nucleotides are removed
Useful regions are rejoined by
ligase enzyme
to
Original Form
336
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
4.
Certain nucleotides are added at the
respectively in eukaryotes. In prokaryotes,
terminal ends enzymatically (terminal
a single RNA polymerase composed of
addition)
different
5.
Transcription of RNA also occurs in the 5-
The RNA molecule may fold on
does
this
work.
3 direction like the replication of DNA.
itself to assume proper shape (folding)
6.
subunits
Some nucleotides may be modified
Translation–
U
(nucleotide modification)
U
After the mRNA has been transported to
Types of RNA
the rough endoplasmic reticulum, it is fed
The three different types of RNA, namely,
into the ribosomal translation machineries.
messenger RNA (mRNA), ribosomal RNA
Ribosomes begins to read the mRNA
(rRNA) and transfer RNA (tRNA) are
sequence from the 5` end to the 3` end. To
transcribed from different regions of the
convert the mRNA into protein, tRNA is
DNA molecule. Three different RNA
used to read the mRNA sequence, 3
polymerases: I, II and III catalyses the
nucleotides at a time. Fig 5 depicts the
transcription of rRNA, mRNA and tRNA
complete process of Translation.
337
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
Fig 4: The mRNA carries the message out of the nucleus to the ribosome in the
0T
0T
cytoplasm where the tRNA helps translate the message to make a protein in cytoplasm
(.https://sites.duke.edu/apep/module-2-the-abcs-of-intoxication/biology-and-chemistryconnections/dna-transcription-translation-synthesis-of-proteins)
338
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
Fig 5: RNA translation a part of protein synthesis
[https://en.wikipedia.org/wiki/Translation_(biology)#/media/File:Protein_synthesis.svg]
339
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
Fig 6 -Translation of mRNA and the synthesis of proteins by a ribosome
(https://en.wikipedia.org/wiki/Translation_(biology)#/media/File:Ribosome_mRNA_translati
32T
on_en.svg)
32T
Ribosome orchestrates the translation of
the tryptic peptides from the soluble
mRNA to synthesize polypeptides, it is
(completed)
helpful to assimilate the following points
were labelled increased with their
[12]-
proximity to the C-terminus, thereby
1. Polypeptide synthesis proceeds from
indicating that incoming amino acids
hemoglobin
the N-terminus to the C-terminus; that
are
is,
polypeptide’s C-terminus.
a
peptidyl
transferase
activity
appends an incoming amino acid to a
2.
appended
Chain
to
elongation
molecules
the
growing
occurs
by
growing polypeptide’s C-terminus. This
linking the growing polypeptide to the
was shown to be the case in 1961 by
incoming tRNA’s amino acid residue:
Howard
exposed
If the growing polypeptide is released
reticulocytes (immature red blood cells)
from the ribosome by treatment with
that
synthesizing
high salt concentrations, its C-terminal
hemoglob into H-labeled leucine for
residue is esterified to a tRNA molecule
less time than it takes to synthesize an
as a peptidyl–tRNA. The nascent
entire polypeptide. The extent to which
(growing) polypeptide must therefore
Dintz
were
is,
actively
who
3
P
P
340
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
grow by being transferred from the
transcription (the nucleus) from the site
peptidyl–tRNA in the P site to the
of translation (the cytosol).
incoming aa–tRNA in the A site to form
a
peptidyl–tRNA
with
one
4. Active
translation
occurs
on
more
polysomes. In both prokaryotes and
residue. After the peptide bond has
eukaryotes, multiple ribosomes can
formed, the new peptidyl–tRNA, which
bind to a single mRNA transcript,
now occupies the A site, is translocated
giving rise to a beads-on-a-string
to the P site so that a new aa–tRNA can
structure
enter the A site. The uncharged tRNA
(polysome) Individual ribosomes are
in the P site moves to the E site before
separated by gaps of 50 to 150 Å so that
it dissociates from the ribosome.
they have a maximum density on the
called
a
polyribosome
3. Ribosomes read mRNA in the 5’to
mRNA of ~1 ribosome per 80 nt.
3’direction: This was shown through
Polysomes arise because once an active
the
protein-
ribosome has cleared its initiation site
synthesizing system in which the
on mRNA, a second ribosome can
mRNA was poly(A) with a 3’-terminal
initiate translation at that site.
use
of
a
cell-free
C: 5’ A-A-A-...-A-A-A-C 3’
P
Ribosomes- Protein Factory
P
Such a system synthesizes a poly
In the early 1950s, Paul Zamecnik et al
(Lys) that has a C-terminal Asn:
conducted an experiment to find out the
Together with the knowledge that AAA
site of protein synthesis. They injected
and AAC code for Lys and Asn and the
radioactive amino acids into rats and then
polarity of peptide synthesis, this
after different time intervals, the liver was
established that the mRNA is read in
removed, homogenized and fractionated
the
by
5’
to
3’
direction.
Because
centrifugation.
The
sub
cellular
mRNA is also synthesized in the 5’ to
fractions were then examined for the
3’ direction; prokaryotic ribosomes can
presence of radioactive protein. After few
commence translation as soon as a
hours or days of the labelled amino acids
nascent mRNA emerges from RNA
injected, all the sub cellular fractions
polymerase. This, however, is not
contained labelled proteins. However,
possible in eukaryotes because the
when
nuclear membrane separates the site of
fractionated only minutes after injection of
the
liver
was
removed
and
the labelled amino acids, labelled protein
341
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
was found only in a fraction containing
Ribosomes
ribonucleoprotein
components: the small ribosomal subunit,
particles,which
were
later named ribosomes.
The ribosome is
0T
0T
0T
a
0T
consist
of
two
major
which reads the RNA, and the large
subunit, which joins amino acids to form
complex molecular
0T
0T32
machine found within all living cells, that
a polypeptide chain.
serves as the site of biological protein
composed of one or more ribosomal RNA
synthesis (translation).
Ribosomes
(rRNA) molecule and a variety of proteins.
link amino acids together in the order
The ribosomes and associated molecules
specified by messenger RNA molecules.
are
0T32
0T
0T32
0T32
0T
Each
subunit
is
0T
0T
0T32
32T
32T
0T32
0T
0T
0T32
0T32
0T
0T
0T32
32T
0T
0T32
also
known
as
the translational
0T
0T
32T
apparatus.
Fig 7 : Ribosomes [http://mol-biol4masters.masters.grkraj.org/html/Protein_Synthesis5Ribosome_as_Translation_Machine.htm]
The sequence of DNA, which encodes the
sequence of amino acids. Amino acids are
sequence of the amino acids in a protein, is
selected, collected, and carried to the
copied into a messenger RNA chain. It
ribosome
may be copied many times into RNA
which enter one part of the ribosome and
chains.
a
bind to the messenger RNA chain. It is
its
during this binding that the correct
sequence for determining the correct
translation of nucleic acid sequence to
0T
0T32
32T
Ribosomes
messenger
RNA
can
chain
bind
and
to
use
342
by transfer
0T
0T32
RNA molecules,
0T32
0T
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
amino acid sequence occurs. For each
resemble each other to a remarkable
coding triplet in the messenger RNA there
degree, evidence of a common origin.
is a distinct transfer RNA that matches and
They differ in their size, sequence,
which carries the correct amino acid for
structure, and the ratio of protein to RNA.
that coding triplet. The attached amino
The
acids are then linked together by another
some antibiotics to
part of the ribosome. Once the protein is
inhibiting their ribosomes, while leaving
produced, it can then fold to produce a
human ribosomes unaffected. In bacteria
specific functional 3-Dstructure although
and archaea, more than one ribosome may
during
move along a single mRNA chain at one
0T
0T32
0T32
synthesis some
0T
differences
0T
proteins start
folding into their correct form.
0T32
0T32
in
structure
kill
0T
allow
bacteria
by
time, each "reading" its sequence and
A ribosome is made from complexes of
producing
RNAs and proteins and is therefore
molecule.
a ribonucleo protein. Each ribosome is
The
divided into two subunits:
eukaryotic
1. a smaller subunit which binds to a
produced from mitochondrial genes, and
larger subunit and the mRNA pattern,
functionally resemble many features of
0T
0T
0T32
0T32
0T32
a
corresponding
protein
0T
32T
ribosomes
in
cells
the mitochondria of
0T
0T32
0T32
(mitoribosomes),
32T
32T
0T
are
those in bacteria, reflecting the likely
2. a larger subunit which binds to the
evolutionary origin of mitochondria. The
tRNA, the amino acids, and the smaller
ribosome is responsible for the synthesis
subunit.
of proteins in cells and is found in all
When a ribosome finishes reading an
cellular organisms. It serves to convert the
mRNA molecule, these two subunits split
instructions found in messenger RNA
apart. Ribosomes are ribozymes, because
(mRNA, which itself is made from
the catalytic peptidyl
instructions in DNA) into the chains of
0T
0T
0T32
that
0T32
links
0T32
32T
transferase activity
0T32
amino-acids that make up proteins. The
RNA.
ribosome is a cellular machine which is
Ribosomes are often embedded in the
highly complex. It is made up of dozens of
intracellular membranes that make up the
distinct proteins (the exact number varies
rough endoplasmic reticulum.
slightly between species) as well as a few
by
acids
0T
is
performed
amino
0T32
the
together
ribosomal
32T
32T
Ribosomesfrom bacteria, archaea and euka
specialized
ryotes (the three domains of life on Earth)
as ribosomal RNA (rRNA). These rRNAs
0T
0T32
0T
0T32
32T
0T
0T32
0T
0T32
0T32
0T
0T
RNA
molecules
known
0T32
0T
32T
343
0T32
0T32
0T
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
do not carry instructions to make specific
Mechanism of Protein Synthesis [8][14]
proteins like mRNAs. The ribosomal
Stage 1: Activation of Amino Acids For
proteins and rRNAs are arranged into two
the synthesis of a polypeptide with a
distinct ribosomal pieces of different size,
defined
known generally as the large and small
chemical requirements must be met: (1)
subunit of the ribosome. Ribosomes
the carboxyl group of each amino acid
consist of two subunits that fit together and
must be activated to facilitate formation of
work as one to translate the mRNA into a
a peptide bond, and (2) a link must be
polypeptide chain during protein synthesis.
established between each new amino acid
Because they are formed from two
and the information in the mRNA that
subunits of non-equal size, they are
encodes it. Both these requirements are
slightly longer in the axis than in diameter.
met by attaching the amino acid to at RNA
Prokaryotic
in the first stage of protein synthesis.
ribosomes
20 nm (200 Å)
0T
0T32
0T32
0T
0T
composed
0T32
32T
of
in
are
diameter
65%
around
and
fundamental
and
tRNA is critical. This reaction takes place
rRNA
Attaching the right amino acid to the right
in the cytosol, not on the ribosome. Each
0T32
proteins.
two
are
35% ribosomal
0T
sequence,
Bacterial ribosomes
are
of the 20 amino acids is covalently
composed of one or two rRNA strands.
attached to a specific tRNA at the expense
Eukaryotic ribosomes contain one or three
of ATP energy, using Mg2+dependent
very large rRNA molecules and multiple
activating enzymes known as amino acyl-
smaller
protein
tRNA synthetases. When attached to their
has
amino acid (amino acylated) the tRNAs
32T
32T
0T32
0T
molecules. Crystallographic work
0T
0T32
0T32
0T
P
P
shown that there are no ribosomal proteins
are said to be “charged.”
close to the reaction site for polypeptide
Stage 2: Initiation The mRNA bearing the
synthesis. This proves that the protein
code for the polypeptide to be made binds
components of ribosomes do not directly
to the smaller of two ribosomal subunits
participate in peptide bond formation
and to the initiating amino acyl-tRNA. The
catalysis, but rather suggests that these
large ribosomal subunit then binds to form
proteins act as a scaffold that may enhance
an initiation complex. The initiating amino
the ability of rRNA to synthesize protein .
acyl- tRNA base pairs
The ribosomal subunits of prokaryotes and
with the mRNA codon AUG that signals
eukaryotes are somehow similar. [13].
the beginning of the polypeptide. This
0T
0T32
0T32
0T
344
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
process, which requires GTP, is promoted
to its corresponding codon in the mRNA.
by cytosolic proteins called initiation
Elongation requires cytosolic proteins
factors.
known as elongation factors. The binding
Stage
3:
Elongation
The
nascent
of each incoming amino acyl-tRNA and
polypeptide is lengthened by covalent
the movement of the ribosome along the
attachment of successive amino acid units,
mRNA are facilitated by the hydrolysis of
each carried to the ribosome and correctly
GTP as each residue is added to the
positioned by its tRNA, which base-pairs
growing polypeptide.
 Amino acids are joined by peptide
The above figure shows,
bond and tRNA is discharged from
 charged tRNA arriving at the A
P site
 D. Peptide chain-carrying tRNA is
site, reading its codon on the
mRNA
translocated to P site, making A
 Amino acid of tRNA at P site is
site free to receive another charged
ready to be transferred to the amino
tRNA
acid of tRNA at A site
Three elongation factors (EF Tu, EF Ts
and EF G) assist in the elongation of the
polypeptide chain. A charged tRNA
345
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
molecule along with its amino acid,
pulled to the P site. This process is called
proline, for example, enters the ribosome
translocation. It requires GTP and a
at the A site. Its anticodon GGA locates
translocase protein called EF-G factor. The
and binds with the complementary codon
GTP is hydrolysed to GDP and inorganic
CCU of mRNA chain by hydrogen bonds.
phosphate (iP) to release energy for the
The amino acid methionine is transferred
process. At this stage, a third tRNA
from its tRNA onto the newly arrived
molecule with its own specific amino acid,
proline tRNA complex where the two
arginine, for example arrives at the A site
amino acids join by a peptide bond. The
of the ribosome and binds with the help of
process is catalyzed by the enzyme
anticodon AGA to the complementary
peptidyl
codon UCU of the mRNA chain. The
transferase
located
on
the
ribosome. In this process, the linkage
dipeptide
between the first amino acid and its tRNA
shifted from the preceding tRNA on the
is broken, and the -COOH group now
third tRNA where it joins the amino acid
forms a peptide bond with the free -NH2
arginine again with the help of peptidyl
group of the second amino acid. Thus, the
transferase enzyme. The dipeptide, thus,
second
tRNA
is
a
dipeptide,
becomes a tripeptide, formyl-methionine-
formylmethionineproline.The
energy
proline-arginine. The second tRNA being
required for the formation of a peptide
now uncharged, leaves the mRNA chain,
bond comes from the free energy released
vacating the P site. The tRNA tripeptide
by
acid
complex is translocated from A site to P
(formylmethionine or methionine) from its
site. The entire process involving arrival of
tRNA.
tRNA-amino acid complex, peptide bond
The first tRNA, now uncharged, separates
formation and translocation is repeated. As
from mRNA chain at the P site of the
the ribosome moves over the mRNA, all
ribosome and returns to the mixed pool of
the codons of mRNA arrive at the A site
tRNAs in the cytoplasm. Here, it is now
one after another, and the peptide chain
available to transport another molecule of
grows. Thus, the amino acids are linked up
its specific amino acid.
into
Now the ribosome moves one codon along
communicated by the DNA through the
the mRNA in the 3 direction. With this,
mRNA. A polypeptide chain which is in
tRNA dipeptide complex at the A site is
the process of synthesis is often called a
separation
carries
formylmethionineproline
of
amino
346
a
polypeptide
in
a
sequence
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
nascent
polypeptide.
growing
Stage 5: Posttranslational Modifications :
polypeptide chain always remains attached
In order to achieve its biologically active
to its original ribosome, and is not
form, the new polypeptide must fold into
transferred from one ribosome to another.
its proper three-dimensional conformation.
Only one polypeptide chain can be
Before
or
after
folding,
the
synthesized at a time on a given ribosome
polypeptide
may
undergo
enzymatic
Stage
Release
processing, including removal of one or
Completion of the polypeptide chain is
more amino acids (usually from the amino
signalled by a termination codon in the
terminus); addition of acetyl, phosphoryl,
mRNA. The new polypeptide is released
methyl, carboxyl, or other groups to
from the ribosome, aided by proteins
certain amino acid residues; proteolytic
called release factors.
cleavage;
At the terminal end of mRNA chain there
oligosaccharides or prosthetic groups.
is a stop, or terminator codon (UAA, UAG
The just released polypeptide is a straight,
or UGA). It is not joined by the anticodon
linear exhibiting a primary molecule,
of any tRNA amino acid complex. Hence,
structure. It may lose some amino acids
there can be no further addition of amino
from the end with the help of a peptidase
acids to the polypeptide chain. The linkage
enzyme, and then coil and fold on itself to
between the last tRNA and the polypeptide
acquire secondary and tertiary structure. It
chain is broken by three release factors.
may
(RF 1, RF 2 and RF 3) and GTP. The
polypeptides, to have quaternary structure.
release is catalyzed by the peptidyl
The
transferase enzyme, the same enzyme that
polysomes are released into the cytoplasm
forms the peptide bonds. The ribosome
and function as structural and enzymatic
jumps off the mRNA chain at the stop
proteins. The proteins formed on the
codon and dissociates into its two subunits.
polysomes attached to ER pass into the ER
The completed polypeptide (amino acid
channels
chain) becomes free in the cytoplasm. The
secretions by exocytosis after packaging in
ribosomes and the tRNAs on release from
the Golgi apparatus.
the mRNA can function again in the same
When the ribosome has moved sufficiently
manner and result in the formation of
down the mRNA chain towards 3 end,
another polypeptide of the same protein.
another ribosome takes up position at the
4:
Termination
The
and
347
and/or
even
proteins
and
attachment
combine
with
synthesized
are
exported
new
of
other
on
as
free
cell
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
initiator codon of mRNA, and starts
produce
synthesis of a second molecule of the same
complementary to the DNA. The RNA
polypeptide chain. At any given time, the
sequence is then translated into the
mRNA chain will, therefore, carry many
corresponding sequence of amino acids to
ribosomes
form
over
which
are
similar
a
an
RNA
protein.
molecule
These
that
transfers
is
of
polypeptide chains of varying length,
biological information are summarized in
shortest near the initiator codon and
the so-called central dogma of molecular
longest near the terminator codon. A row
biology formulated by Crick in 1958.Just
of ribosomes
the mRNA
as the daughter strands of DNA are
molecule, is called a polyribosome, or a
synthesized from free deoxynucleoside
polysome. Synthesis of many molecules of
triphosphates that pair with bases in the
the same polypeptide simultaneously from
parent DNA strand, RNA strands are
one mRNA molecule by a polysome is
synthesized
called translational amplification.
triphosphates
Genes instruct when protein would be
Synthesis
complementary bases in one DNA strand
In experiments with the mold Neurospora
protein-coding gene (called messenger
crassa in the 1940s, George Beadle and
RNA, or mRNA) makes its way to a
Edward Tatum found that there is a
ribosome, an organelle that is itself
specific connection between genes and
composed largely of RNA (ribosomal
enzymes, the one gene–one enzyme theory.
RNA, or rRNA). At the ribosome, each set
Beadle and Tatum showed that mutant
of three nucleotides inthe mRNA pairs
varieties
were
with three complementary nucleotides in a
generated by irradiation with X-rays
small RNA molecule called a transfer
required additional nutrients in order to
RNA, or tRNA. Attached to each tRNA
grow. Presumably, the offspring of the
molecule is its corresponding amino acid.
radiation-damaged cells lacked the specific
The ribosome catalyzes the joining of
enzymes necessary to synthesize those
amino acids, which are the monomeric
nutrients.
units of proteins. Amino acids are added to
The link between DNA and enzymes
the growing protein chain according to the
(nearly all of which are proteins) is RNA.
order in which the tRNA molecules bind to
The DNA of a gene is transcribed to
the mRNA. Since the nucleotide sequence
of
joined to
Neurospora
that
from
that
free
pair
ribonucleoside
with
the
of a gene. The RNA that corresponds to a
348
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
of the mRNA in turn reflects the sequences
your genes respond to also includes your
of nucleotides in the gene, DNA directs the
conscious
synthesis of proteins. It follows that
unconscious beliefs.
alterations to the genetic material of an
Science has indeed taken us far beyond
organism
manifest
Newtonian physics, which says you live in
altered
a mechanical universe. According to this
structures and functions. Researchers can
belief, your body is just a biological
compile a catalog of all the information
machine, so by modifying the parts of the
encoded in an organism’s DNA. The study
machine, we can modify our health. Also,
of the genome’s size, organization, and
as a biological machine, our body is
gene content is known as genomics. By
thought to respond to physical "things"
analogy, transcriptomics refers to the study
like the active chemicals in drugs, and by
of gene expression, which focuses on the
adjusting the drugs that modify our
set of mRNA molecules, or transcriptome,
machinery, doctors can modify and control
that is transcribed from DNA under any
health. However, with the advent of
particular set of circumstances. Finally,
quantum physics, scientists have realized
proteomics is the study of the proteins (the
the flaws in Newtonian physics, as
proteome)
of
quantum physics shows us that the
transcription and translation. Although an
invisible, immaterial realm is actually far
organism’s genome remains essentially
more important than the material realm. In
unchanged throughout its lifetime, its
fact,
transcriptome and proteome may vary
environment far more than physical matter.
significantly among different types of
According to Cellular biologist Bruce
tissues,
Lipton the true secret to life does not lie
(mutations)
themselves
as
may
proteins
produced
as
developmental
with
a
result
stages,
and
our
thoughts,
thoughts
emotions,
may
shape
and
our
environmental conditions [12].
within our DNA, but rather within the
Emotions also change the path of
mechanisms of your cell membrane. Each
Genetic information [15]
cell membrane has receptors that pick up
Scientific research shows that as if genes
various environmental signals, and this
changing
to
mechanism controls the "reading" of the
environmental factors such as nutrients
genes inside your cells. Our cells can
wasn't enough, other researchers have
choose to read or not read the genetic
demonstrated that this "environment" that
blueprint depending on the signals being
expression
in
response
349
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
received from the environment. So having
connection between genetics and disease
a "cancer program" in your DNA does not
have been stymied by their inability to find
automatically mean you're destined to get
strong
cancer. This genetic information does not
variation and risk for most common
ever have to be expressed. What this all
diseases, leading researchers to wonder
means is that we are not controlled by your
where the 'missing heritability' is hiding.
genetic makeup. Instead, our genetic
The new study at least provides one place
readout (which genes are turned "on" and
to look.
connections
between
genetic
which are turned "off") is primarily
Conclusion and Discussion
determined by your thoughts, attitudes,
and perceptions.
Literature shows that in Vedic time or in
ancient India (Aryavrat, Bharat ancient
Editing the central dogma
names of India ) “Sadhus”, “Mahatmas”
According to the Nature [16], research the
and even Gods have power to change in
central dogma says that there is faithful
complete organism into another organism.
transcription of DNA into RNA. This
When we review scientific literatures and
challenges that idea on a much larger scale
researches we studied that by yoga,
than was known. The work suggests that
meditation and chanting of Vedic mantras
RNA editing is providing a previously
written in Samveda, Yujurveda, Atherveda
unappreciated source of human genetic
and Rigveda we modify our genetic codes,
diversity that could affect, for instance,
DNA sequence and the process of central
how vulnerable different people are to
dogma also. By modifying genetic codes
disease. Research article published in
and DNA we connect to supreme powers
Science [17] shows that not know whether
or attain divine powers which we have
there are heritable changes, passed down
seen in every era or Yuga whether it
from parent to child, that affect how much
is Satya Yuga, Treta Yuga , Dvapara
RNA editing occurs in different people.
Yuga and also in Kali Yuga. One among in
But scientists already know of a handful of
thousands attain such type of powers this
RNA editing proteins that play a role in
was mentioned in Shrimad Bhagwad Gita
human health, such as the APOBEC
in Chapter 7 verse 3.
32T
0T32
32T
enzymes, some of which have antiviral
activity. Researchers investigating the
350
0T
32T
32T
0T32
0T
32T
32T
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
nothing else can do it. Central Dogma has
proved a fruitful principle, ever since
James Watson and Crick discovered the
double helix structure of DNA in the
1950s. DNA is the blueprint, it gives
These types of
“Sidhiya” or “Shaktiya”
instructions to the RNA and to protein it
are not situated outside our body but
about how to arrange themselves. The
outside environment influence the cell
whole changing process starts from here
metabolism. These all are happen due to
when we modify the instructions path from
the cell signalling process of particular
DNA the whole body get converted into
cell. According to Francis Crick, the co-
another. Our body is nothing but a well-
discoverer of the structure of DNA,
mannered organization of proteins which
prepared a genetic principle which he
are formed by the codes of DNA and
entitled, “The Central Dogma”. The
carried by RNA to form these proteins.
transfer of
information from nucleic acid
Every living being on the earth whether
to nucleic acid or from nucleic acid to
plants or animal species; are made up
protein may be possible. But vice versa is
proteins only that depends on DNA. If it is
not possible. All this process of changing
possible to change the codes of DNA
the structure of organism into another is
through yoga or meditation then the RNA
governed by Central Dogma. The central
will carry the coded information for the
dogma is an important scientific process.
formation of corresponding protein and if
The complex coding within the DNA in
the proteins would be changed then the
the cell nucleus decides the trait for the
entire morphology would change. Not only
organism. Species cannot change from one
yoga and meditation but the external
into another species. All the members in a
environment is also responsible for such
species can only be the outcome of the
type of changes. According to Nature and
wide range of “gene pool” data in the
one scientific article it is mentioned that
DNA, but no member of that species can,
outside environment [15] can also edit [16]
because of the environment or what has
the process of Central dogma to produce
happened to that individual, changes into
new protein. It means that science accepts
another species. Only change in the DNA
the fact that the process of central dogma
coding can produce such changes [18];
can be edited to form new proteins. But
351
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
science doesn’t tells that what type of
At last on the behalf of scientific literature
proteins would be formed finally, this
shown in this paper and other researches
concept is cleared by religious texts that if
we conclude that by changing the DNA
a specified amount of DNA codes are
codes and diverting the information path of
changed
physical
Central Dogma we can change the
morphology of an organism can change
organism structure as we know that
from one species to the other.
majority of the body constitutes different
then
the
entire
types of protein.
10 heads of Ravana, Panchmukhi of Lord
Hanuman, enlarged body (viraat roop)
form of Lord Krishna and similar type of
Acknowledgement
texts show that everything in a living body
Authors are thankful to Lord Shri Hari
is determined by the proteins only. All
Vishnu for providing us knowledge to
these things are the higher level of science
work on these types of work. Authors are
mentioned in religious scriptures, which
also thankful to Mr. Brahampal Singh
we call “Chamatkaar”. In actual state, this
(Aghera), Advocate, Chamber No G-6,
is not any “Chamatkaar” but a scientific
process
called
“central
dogma
Law Chamber Building, Meerut, U.P.,
of
India
molecular biology” in which the code from
for
people used to do such things, there was
1. https://publications.nigms.nih.gov/s
not any name given to any process but
with
the
tremendous
Literature Quoted:
protein synthesis. In previous time when
along
us
knowledge on concern topic.
the DNA is the controller of the entire
currently
providing
tructlife/chapter1.html#code
scientific
2. The chemical building block of
researches different process were given
life http://www.mhhe.com/biosci/g
32T
specified scientific names. During various
enbio
researches, the role of proteins was also
/raven6b/graphics/raven06b/other/r
determined that they help in the formation
aven06b_03.pdf
32T
of a living being and may be this is the
3. http://www.jagran.com/photogaller
32T
reason
proteins
are
known
as
the
y-13972-2.html#photodetail
32T
“building blocks”.
4. Judson H.F. 1979. The Eighth Day
of
352
Creation:
Makers
of
the
International Journal of Scientific Engineering and Applied Science (IJSEAS) - Volume-2, Issue-5, May 2016
ISSN: 2395-3470
www.ijseas.com
12. Donald Voet, Judith G. Voet,
Revolution in Biology. Simon and
Charlotte W. Pratt, Fundament of
Schuster. NewYork.
protein
Biochemistry, 3rd Edition, John
synthesis. Symp. Soc. Exp. Biol.
Wiley and Sons, Inc, 2008, Printed
12: 138–163.
in United States of America.
5. Crick
F.H.
1958.
On
P
6. Crick F. 1970. Central dogma of
P
13. https://en.wikipedia.org/wiki/Ribos
molecular biology. Nature 227:
ome
561–563.
14. David L. Nelson and Michael M.
7. James A. Shapiro. 2009, Revisiting
Cox,
Lehninger
the Central Dogma in the 21st
Biochemistry,
Century.
website
Natural
Genetic
Principles
Fourth
of
Edition,
Engineering and Natural Genome
www.whfreeman.com/lehninger4e
Editing: Ann. N.Y. Acad. Sci.
15. http://articles.mercola.com/sites/art
32T
icles/archive/2012/04/11/epigenetic
1178: 6–28.
-vs-determinism.aspx
8. Transcription – translation - genetic
code
and
outline
of
32T
16. http://www.nature.com/news/2011/
protein
synthesis http://agridr.in/tnauEAgri
110519/full/news.2011.304.html
32T
/eagri50/GBPR111/lec17.pdf
17. Mingyao Li, Isabel X. Wang, Yun
32T
9. http://www.cbs.dtu.dk/courses/gen
Li,
Alan
Bruzel,
Allison
L.
omics_course/roanoke/genetics980
Richards, Jonathan M. Toung,
320f.htm
Vivian
10. http://www.britannica.com/science/
G.
Widespread
32T
endoplasmic-reticulum#ref90894
Sequence
32T
Cheung
RNA
(2011).,
and
Differences
DNA
in
the
Human Transcriptome, SCIENCE ,
11. https://sites.google.com/site/gacrct
32T
eoctsciencewholegroup/home/eoct-
VOL 333, pg 53-58
18. Vance Ferrell (2006), Science vs
science-whole-group-wikisites/04_biology_genetics-and-
Evolution, Published by Evolution
heredity
Facts,
32T
Inc.,
United
States
of
America, www.evolution-facts.org
32T
353
32T