Translation termination in eukaryotes: polypeptide release factor eRF1 is composed of functionally and structurally distinct domains - Wikidata - awgldk - TriplyDB

Translation termination in eukaryotes: polypeptide release factor eRF1 is composed of functionally and structurally distinct domains

Translation termination in eukaryotes: polypeptide release factor eRF1 is composed of functionally and structurally distinct domains

http://www.wikidata.org/entity/Q34362482

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Interactions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways The invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosome Invariant amino acids essential for decoding function of polypeptide release factor eRF1.Termination of translation: interplay of mRNA, rRNAs and release factors?NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor Viable nonsense mutants for the essential gene SUP45 of Saccharomyces cerevisiae Translational readthrough potential of natural termination codons in eucaryotes--The impact of RNA sequence Eukaryotic class 1 translation termination factor eRF1--the NMR structure and dynamics of the middle domain involved in triggering ribosome-dependent peptidyl-tRNA hydrolysis Structural insights into eRF3 and stop codon recognition by eRF1 Omnipotent role of archaeal elongation factor 1 alpha (EF1 ) in translational elongation and termination, and quality control of protein synthesis Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1 Fine-tuning of translation termination efficiency in Saccharomyces cerevisiae involves two factors in close proximity to the exit tunnel of the ribosome.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.Stop codon recognition in ciliates: Euplotes release factor does not respond to reassigned UGA codon Structural characterization of eRF1 mutants indicate a complex mechanism of stop codon recognition Mutation at tyrosine in AMLRY (GILRY like) motif of yeast eRF1 on nonsense codons suppression and binding affinity to eRF3.Molecular dissection of translation termination mechanism identifies two new critical regions in eRF1.Omnipotent decoding potential resides in eukaryotic translation termination factor eRF1 of variant-code organisms and is modulated by the interactions of amino acid sequences within domain 1.The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors.Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.Mouse GSPT2, but not GSPT1, can substitute for yeast eRF3 in vivo.Class I release factors in ciliates with variant genetic codes Suppression of eukaryotic translation termination by selected RNAs.Inhibition of translation termination mediated by an interaction of eukaryotic release factor 1 with a nascent peptidyl-tRNA.Efficient assembly and annotation of the transcriptome of catfish by RNA-Seq analysis of a doubled haploid homozygote Comparison of characteristics and function of translation termination signals between and within prokaryotic and eukaryotic organisms Distinct paths to stop codon reassignment by the variant-code organisms Tetrahymena and Euplotes.Assessing functional divergence in EF-1alpha and its paralogs in eukaryotes and archaebacteria Chemical footprinting reveals conformational changes of 18S and 28S rRNAs at different steps of translation termination on the human ribosome.Connection between stop codon reassignment and frequent use of shifty stop frameshifting Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1.Adenine and guanine recognition of stop codon is mediated by different N domain conformations of translation termination factor eRF1.The ribosomal A site-bound sense and stop codons are similarly positioned towards the A1823-A1824 dinucleotide of the 18S ribosomal RNA.Class-1 translation termination factors: invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition Convergence and constraint in eukaryotic release factor 1 (eRF1) domain 1: the evolution of stop codon specificity.GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation termination.Antizyme frameshifting as a functional probe of eukaryotic translational termination.Two-step model of stop codon recognition by eukaryotic release factor eRF1 In Aspergillus nidulans the suppressors suaA and suaC code for release factors eRF1 and eRF3 and suaD codes for a glutamine tRNA.

P2860

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P2860

Translation termination in eukaryotes: polypeptide release factor eRF1 is composed of functionally and structurally distinct domains

http://www.wikidata.org/entity/Q34362482

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2000 nî lūn-bûn

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2000 թուականի Մարտին հրատարակուած գիտական յօդուած

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2000 թվականի մարտին հրատարակված գիտական հոդված

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2000年の論文

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2000年論文

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Frolova LY

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Kisselev LL

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Merkulova TI

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P2860

Molecular cloning of a novel member of the eukaryotic polypeptide chain-releasing factors (eRF). Its identification as eRF3 interacting with eRF1

Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity

The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae

Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation.

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

C-terminal domains of human translation termination factors eRF1 and eRF3 mediate their in vivo interaction

Direct recognition of mRNA stop signals by Escherichia coli polypeptide chain release factor two

Escherichia coli release factor 3: resolving the paradox of a typical G protein structure and atypical function with guanine nucleotides.

Release factors differing in specificity for terminator codons

Identification of the prfC gene, which encodes peptide-chain-release factor 3 of Escherichia coli

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