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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