A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation. - Wikidata - awgldk - TriplyDB

A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation.

A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation.

http://www.wikidata.org/entity/Q30634770

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HemK2 protein, encoded on human chromosome 21, methylates translation termination factor eRF1 Termination of translation: interplay of mRNA, rRNAs and release factors?Recognition of ribosomal protein L11 by the protein trimethyltransferase PrmA Release Factors 2 from Escherichia coli and Thermus thermophilus: structural, spectroscopic and microcalorimetric studies Eukaryotic class 1 translation termination factor eRF1--the NMR structure and dynamics of the middle domain involved in triggering ribosome-dependent peptidyl-tRNA hydrolysis Insights into Translational Termination from the Structure of RF2 Bound to the Ribosome Structure of the 70S ribosome bound to release factor 2 and a substrate analog provides insights into catalysis of peptide release Recognition of the amber UAG stop codon by release factor RF1 Mechanism of activation of methyltransferases involved in translation by the Trm112 'hub' protein The zinc finger protein Ynr046w is plurifunctional and a component of the eRF1 methyltransferase in yeast.The yeast translation release factors Mrf1p and Sup45p (eRF1) are methylated, respectively, by the methyltransferases Mtq1p and Mtq2p.The glutamine residue of the conserved GGQ motif in Saccharomyces cerevisiae release factor eRF1 is methylated by the product of the YDR140w gene.Mapping functionally important motifs SPF and GGQ of the decoding release factor RF2 to the Escherichia coli ribosome by hydroxyl radical footprinting. Implications for macromolecular mimicry and structural changes in RF2 The N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase PrmC/HemK in Chlamydia trachomatis methylates class 1 release factors Histidine methylation of yeast ribosomal protein Rpl3p is required for proper 60S subunit assembly.HemK, a class of protein methyl transferase with similarity to DNA methyl transferases, methylates polypeptide chain release factors, and hemK knockout induces defects in translational termination.Polypeptide release at sense and noncognate stop codons by localized charge-exchange alterations in translational release factors.tRNA mimicry in translation termination and beyond.The methylator meets the terminator Stop codons preceded by rare arginine codons are efficient determinants of SsrA tagging in Escherichia coli.The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors.Deficiency in a glutamine-specific methyltransferase for release factor causes mouse embryonic lethality.Inactivation of the RluD pseudouridine synthase has minimal effects on growth and ribosome function in wild-type Escherichia coli and Salmonella enterica.Comparison of characteristics and function of translation termination signals between and within prokaryotic and eukaryotic organisms Deletion of the RluD pseudouridine synthase promotes SsrA peptide tagging of ribosomal protein S7 Two groups of phenylalanine biosynthetic operon leader peptides genes: a high level of apparently incidental frameshifting in decoding Escherichia coli pheL.Ribosome excursions during mRNA translocation mediate broad branching of frameshift pathways Substrate Specificity of the HEMK2 Protein Glutamine Methyltransferase and Identification of Novel Substrates Release factor one is nonessential in Escherichia coli.Global analysis of translation termination in E. coli.Translation factors direct intrinsic ribosome dynamics during translation termination and ribosome recycling.Identification of novel virulence-associated genes via genome analysis of hypothetical genes.Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase Uniformity of Peptide Release Is Maintained by Methylation of Release Factors.The Expression of Antibiotic Resistance Methyltransferase Correlates with mRNA Stability Independently of Ribosome Stalling.Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus.Structural aspects of translation termination on the ribosome.A highly purified, fluorescently labeled in vitro translation system for single-molecule studies of protein synthesis.Bacterial Protein Synthesis as a Target for Antibiotic Inhibition.Structural basis of co-translational quality control by ArfA and RF2 bound to ribosome.

P2860

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P2860

A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation.

http://www.wikidata.org/entity/Q30634770

description

2000 nî lūn-bûn

@nan

2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2000年の論文

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年學術文章

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name

A post-translational modificat ...... es termination of translation.

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A post-translational modificat ...... es termination of translation.

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type

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A post-translational modificat ...... es termination of translation.

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A post-translational modificat ...... es termination of translation.

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A post-translational modificat ...... es termination of translation.

@ast

A post-translational modificat ...... es termination of translation.

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P1433

The EMBO Journal

P1476

A post-translational modificat ...... es termination of translation.

@en

P2093

A Engström

http://www.w3.org/2001/XMLSchema#string

L Mora

http://www.w3.org/2001/XMLSchema#string

V Dinçbas-Renqvist

http://www.w3.org/2001/XMLSchema#string

V Heurgué-Hamard

http://www.w3.org/2001/XMLSchema#string

P2860

DNA sequencing with chain-terminating inhibitors

A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor

The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis

Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes

Release factor RF3 in E.coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner

Peptide bond formation by in vitro selected ribozymes.

Origins of minigene-dependent growth inhibition in bacterial cells.

Shutdown in protein synthesis due to the expression of mini-genes in bacteria.

A direct estimation of the context effect on the efficiency of termination.

Autogenous suppression of an opal mutation in the gene encoding peptide chain release factor 2.

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6900-6907

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scholarly article

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10.1093/EMBOJ/19.24.6900

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24

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19

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Richard H. Buckingham

Måns Ehrenberg

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2000-12-01T00:00:00Z

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12210760

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11118225

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P921

Escherichia coli

P932

305885

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