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Transcription Translation PowerPoint
Transcription Translation PowerPoint

... 1. Cutting out certain ____ during processing gives tRNA its ____ shape. 2. The anticodon on tRNA is complimentary to the ____ on mRNA. 3. Why does tRNA have an amino acid binding site? (What is tRNA’s function?) ...
Protein Purification
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... Now a team from EMBL Heidelberg and Stanford University led by Lars Steinmetz has turned this on its head. The researchers have shown that one end of the mRNA begins to decay while the other is still serving as a template for protein production. Thus, studying the decaying mRNA also provides a snaps ...
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2005 MCB 3020 Study Objectives, Part 2
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Shaping the Endoplasmic Reticulum into a Social Network
Shaping the Endoplasmic Reticulum into a Social Network

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Proteomics methods for subcellular proteome analysis
Proteomics methods for subcellular proteome analysis

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The families of pathogenesis-related proteins, their activities, and

... activities that are present in many, and perhaps all, plant species [10]. In a number of plant species, a strong induction of genes encoding either thionins, plant defensins or LPTs has been observed upon infection of the leaves by pathogens. Hence, at least some of these antimicrobial peptides must ...
Genetic Code, RNA and Protein Synthesis
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Digestive Enzymes - Goshen Cancer Survivor Network
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Essential Cell Biology Chapter 4 excerpt
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RNA Processing: Eukaryotic mRNAs
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... • There is an intranuclear protein/RNA complex called the splicosome that ensures proper splicing. • Three types of short sequences dictate the precise cutting of the intron/exon boundaries - called splice junctions. – Splice donor: 5’ end of intron: exon-G-U – Splice Acceptor: 3’ end of intron: A-G ...
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Intrinsically Disordered Proteins as Drug Targets
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... regulation of amino acid metabolism (2– 4) (Fig. 1). These include both metabolic enzymes and transcription regulators. In fact, the expression of some ACT-containing enzymes is under the control of ACT-containing transcription regulators. This has resulted in the ACT domain being referred to as “th ...
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... Late embryogenesis abundant (LEA) proteins were first identified and characterized in cotton and wheat during the last stage of seed maturation (Galau and Hughes 1987). Up to 4 % of total cellular proteins during seed development are LEA proteins (Roberts et al. 1993). LEA proteins are grouped into ...
Apoptosis of Lung Epithelial Cells in Response to Meconium and
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... resuspended in ice-cold buffer (20 mM HEPES, pH 7.0, 50 mM NaCl and 1 mM EDTA), and centrifuged at 21,000g (4oC ) for 15 minutes. Proteins were isolated from cell extract using acetone precipitation and then purified to homogeneity on a Sephadex G100 column (2cm x 50cm), equilibrated with 0.05M sodi ...
(mRNA). - canesbio
(mRNA). - canesbio

... – They seem to facilitate the export of mRNA – They protect mRNA from hydrolytic enzymes – They help ribosomes attach to the 5 end ...
檔案下載 - 國立宜蘭大學生物技術與動物科學系
檔案下載 - 國立宜蘭大學生物技術與動物科學系

... Copyright © 2009 Pearson Education, Inc. ...
Transcription
Transcription

... Gene specific regulatory proteins (factors) Specific transcription factors - proteins that bind to specific regulatory DNA sequences (enhancers, silencers, HRE) lying on the same chromosome, distant from promoters (very often in large distance). They act as activators or repressors of the given gen ...
Regulation of cellular homoeostasis by reversible lysine acetylation
Regulation of cellular homoeostasis by reversible lysine acetylation

... three basic factors: (i) the current activity of its specific acetyltransferase(s), (ii) the current activity of its deacetylase(s), and (iii) the availability of acetylCoA as an acetylation substrate. Adding another layer of complexity is the fact that proteins may contain multiple lysine residues, ...
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SR protein



SR proteins are a conserved family of proteins involved in RNA splicing. SR proteins are named because they contain a protein domain with long repeats of serine and arginine amino acid residues, whose standard abbreviations are ""S"" and ""R"" respectively. SR proteins are 50-300 amino acids in length and composed of two domains, the RNA recognition motif (RRM) region and the RS binding domain. SR proteins are more commonly found in the nucleus than the cytoplasm, but several SR proteins are known to shuttle between the nucleus and the cytoplasm.SR proteins were discovered in the 1990s in Drosophila and in amphibian oocytes, and later in humans. In general, metazoans appear to have SR proteins and unicellular organisms lack SR proteins.SR proteins are important in constitutive and alternative pre-mRNA splicing, mRNA export, genome stabilization, nonsense-mediated decay, and translation. SR proteins alternatively splice pre-mRNA by preferentially selecting different splice sites on the pre-mRNA strands to create multiple mRNA transcripts from one pre-mRNA transcript. Once splicing is complete the SR protein may or may not remain attached to help shuttle the mRNA strand out of the nucleus. As RNA Polymerase II is transcribing DNA into RNA, SR proteins attach to newly made pre-mRNA to prevent the pre-mRNA from binding to the coding DNA strand to increase genome stabilization. Topoisomerase I and SR proteins also interact to increase genome stabilization. SR proteins can control the concentrations of specific mRNA that is successfully translated into protein by selecting for nonsense-mediated decay codons during alternative splicing. SR proteins can alternatively splice NMD codons into its own mRNA transcript to auto-regulate the concentration of SR proteins. Through the mTOR pathway and interactions with polyribosomes, SR proteins can increase translation of mRNA.Ataxia telangiectasia, neurofibromatosis type 1, several cancers, HIV-1, and spinal muscular atrophy have all been linked to alternative splicing by SR proteins.
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