Single amino acid substitution in prokaryote polypeptide release factor 2 permits it to terminate translation at all three stop codons.
about
Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switchInsights into Translational Termination from the Structure of RF2 Bound to the RibosomeMapping 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 RF2Polypeptide release factors and stop codon recognition in the apicoplast and mitochondrion of Plasmodium falciparumThermodynamic and kinetic insights into stop codon recognition by release factor 1.Diverse bacterial genomes encode an operon of two genes, one of which is an unusual class-I release factor that potentially recognizes atypical mRNA signals other than normal stop codonsMutation at tyrosine in AMLRY (GILRY like) motif of yeast eRF1 on nonsense codons suppression and binding affinity to eRF3.Polypeptide release at sense and noncognate stop codons by localized charge-exchange alterations in translational release factors.tRNA mimicry in translation termination and beyond.Specific bonding of puromycin to full-length protein at the C-terminus.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.Translation termination in eukaryotes: polypeptide release factor eRF1 is composed of functionally and structurally distinct domainsA tripeptide discriminator for stop codon recognition.Evolutionary conservation of reactions in translationProtein tRNA mimicry in translation termination.RF1 knockout allows ribosomal incorporation of unnatural amino acids at multiple sites.Determination of the core of a minimal bacterial gene setRelease factor one is nonessential in Escherichia coli.Experimental Evolution of Escherichia coli Harboring an Ancient Translation ProteinStructural aspects of translation termination on the ribosome.Enhancement of the synthesis of RpoN, Cra, and H-NS by polyamines at the level of translation in Escherichia coli cultured with glucose and glutamate.Overcoming Challenges in Engineering the Genetic CodeRewriting the Genetic Code.Peptide release promoted by methylated RF2 and ArfA in nonstop translation is achieved by an induced-fit mechanismHighly reproductive Escherichia coli cells with no specific assignment to the UAG codon.Near-cognate suppression of amber, opal and quadruplet codons competes with aminoacyl-tRNAPyl for genetic code expansion.Functional Constraints on Replacing an Essential Gene with Its Ancient and Modern HomologsThe codon specificity of eubacterial release factors is determined by the sequence and size of the recognition loop.A genetic approach for analyzing the co-operative function of the tRNA mimicry complex, eRF1/eRF3, in translation termination on the ribosome.Efficient decoding of the UAG triplet as a full-fledged sense codon enhances the growth of a prfA-deficient strain of Escherichia coli.Release factor 2 frameshifting sites in different bacteria.Enhancement of the synthesis of RpoE and StpA by polyamines at the level of translation in escherichia coli under heat shock conditions.C-terminal interaction of translational release factors eRF1 and eRF3 of fission yeast: G-domain uncoupled binding and the role of conserved amino acids.Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis.Enhancement of +1 frameshift by polyamines during translation of polypeptide release factor 2 in Escherichia coli.Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release.How protein reads the stop codon and terminates translation.R213I mutation in release factor 2 (RF2) is one step forward for engineering an omnipotent release factor in bacteria Escherichia coli.Polypeptide release factor eRF1 from Tetrahymena thermophila: cDNA cloning, purification and complex formation with yeast eRF3.Amber (UAG) suppressors affected in UGA/UAA-specific polypeptide release factor 2 of bacteria: genetic prediction of initial binding to ribosome preceding stop codon recognition.
P2860
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P2860
Single amino acid substitution in prokaryote polypeptide release factor 2 permits it to terminate translation at all three stop codons.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Single amino acid substitution ...... tion at all three stop codons.
@ast
Single amino acid substitution ...... tion at all three stop codons.
@en
type
label
Single amino acid substitution ...... tion at all three stop codons.
@ast
Single amino acid substitution ...... tion at all three stop codons.
@en
prefLabel
Single amino acid substitution ...... tion at all three stop codons.
@ast
Single amino acid substitution ...... tion at all three stop codons.
@en
P2093
P2860
P356
P1476
Single amino acid substitution ...... tion at all three stop codons.
@en
P2093
P2860
P304
P356
10.1073/PNAS.95.14.8165
P407
P577
1998-07-01T00:00:00Z