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SHORT COMMUNICATION Why Are Both Ends of the Polypeptide
SHORT COMMUNICATION Why Are Both Ends of the Polypeptide

... synthesized has a fixed time frame to fold. If no stable 3D arrangement is found within that time span (⬃0.1 s), then a new round of possible conformations will be tried because the polypeptide has been elongated by one amino acid. Such a procedure of protein folding appears more attractive (both for ...
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... the tumour cells, lead to the decay of the tumour mass. Saimiri sciureus monkeys, the natural hosts, are lifelong virus carriers following inapparent infection early in life. Virus can be isolated from lymphocytes after co-cultivation in vitro with susceptible cells or directly from throat swabs of ...
The Roles of Moonlighting Proteins in Bacteria
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... mutant adhered poorly to human pharyngeal cells, bound significantly less with human plasminogen, and lost its innate antiphagocytic activity (Boël et al., 2005). More importantly, the mutant was completely attenuated for virulence in a mouse peritonitis model (Jin et al., 2011). This result was the ...
Transmembrane domains control exclusion of membrane proteins
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... membrane proteins. We used CD1b as a reporter protein because this protein normally traffics through endocytic compartments (Jackman et al., 1998) and thus should not be sensitive to proteases found in endosomal compartments. Indeed, we have observed that both CD1b and its specific monoclonal antibo ...
File S4 - G3: Genes | Genomes | Genetics
File S4 - G3: Genes | Genomes | Genetics

... involving distinct mechanisms both in the cytoplasm and the nucleus. In the case of fne, two mechanistically distinct presumptive scenarios could explain our data. The sequence motif UUUUUUAUCUCUUUUU lies 17 nucleotides downstream of the 5’ splice site generating fne-a transcripts and 159 nt upstre ...
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... roughly logarithmic function of its frequency in the MSA.9 Indeed, approaches based on this idea have proven broadly successful at creating more stable proteins.5;6;10 However, because the sequences of natural proteins generally derive from a common ancestor, they tend to be heavily biased by evolut ...
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... • The CAP-cAMP complex stimulates transcription of the lac operon by binding to an activator site adjacent to the promoter and helping RNA polymerase to bind to the promoter. This closed complex then converts to an open promoter complex. CAP-cAMP causes recruitment through protein-protein interactio ...
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... pl//about.htm) on proteins of the Swiss-Prot database (version 42) (Bairoch and Apweiler, 1999). We created the dataset of experimentally verified segments including the 9-amino acid long sequence fragments (positive instances). We built the dataset of negative cases (negative instances) in order to ...
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... does not contain the full-length cDNA as it lacks both the start and stop codons. Rescreening the mantle cDNA library with a DIG-labeled insert from clone 1 resulted in the identification of 15 positive clones from approximately one million clones. DNA was extracted from all 15 clones, and restricti ...
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... The plasmids used were pCG-M(ED), pCG-M(ED89KAE), pCGM(WTF) and pCG-M(WTF89EAK). They were generated in pCG(DC), a modified eukaryotic expression vector which contains the cytomegalovirus immediate-early promoter and DraI and CspI restriction sites. These sites facilitate the directional cloning of ...
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... A region of a DNA molecule that indicates to an enzyme where to bind to make RNA is the ...
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...  At least 61 different forms each has a specific anticodon as part of its structure.  tRNA “translates” the message on the mRNA into a polypeptide chain ...
DNA transcription 3.lecture ENG OK
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... nucleotides in length) and more than 50 proteins. Each of the snRNA molecules is attached to specific proteins to form small nuclear ribonucleoproteinssnurps (snRNPs), called U1, U2, U4, U5 and U6. snRNPs contribute to the process of splicing by recognizing sequences in the mRNA or promoting rearran ...
The Diversity of Lysine-Acetylated Proteins in Escherichia coli
The Diversity of Lysine-Acetylated Proteins in Escherichia coli

... Lysine acetylation is a reversible and highly regulated posttranslational modification. Since histone acetylation was discovered in 1968 [20], many lysine-acetylated histone and nonhistone proteins have been identified in eukaryotes, and this modification regulates diverse protein properties includi ...
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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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