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Article

Suppression of temperature-sensitive defects of polypeptide release factors RF-1 and RF-2 by mutations or by an excess of RF-3 in Escherichia coli.

Journal of molecular biology - 17 May 1996

Matsumura K, Ito K, Kawazu Y, Mikuni O, Nakamura Y

Abstract excerpt

The termination of protein synthesis in bacteria requires two codon-specific polypeptide-release factors, RF-1 and RF-2. A third factor, RF-3, stimulates the RF-1 and RF-2 activities in vitro. To clarify the in vivo role of RF-3 for the RF-2 dependent termination, we isolated and characterized suppressor mutations for the temperature-sensitive RF-2 mutation prfB286. One of the intergenic suppressor mutations,...

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Identifiers

PMID: 8636994
DOI: 10.1006/jmbi.1996.0271

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Related research

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Research trail→

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Suppression of temperature-sensitive defects of polypeptide release factors RF-1 and RF-2 by mutations or by an excess of RF-3 in Escherichia coli.PMID 8636994Read ↗

A novel class of bacterial translation factor RF3 mutations suggests specific structural domains for premature peptidyl-tRNA drop-off.Semantic proximity Read ↗

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Stop codon recognition and interactions with peptide release factor RF3 of truncated and chimeric RF1 and RF2 from Escherichia coli.Semantic proximity Read ↗

Sequence and functional analysis of mutations in the gene encoding peptide-chain-release factor 2 of Escherichia coli.Semantic proximity Read ↗

Global analysis of translation termination in E. coli.Semantic proximity Read ↗

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Ribosomal protein L11 mutations in two functional domains equally affect release factors 1 and 2 activity.Semantic proximity Read ↗

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Ribosome release factor RF4 and termination factor RF3 are involved in dissociation of peptidyl-tRNA from the ribosome.Semantic proximity Read ↗

Temperature sensitivity caused by mutant release factor 1 is suppressed by mutations that affect 16S rRNA maturation.Semantic proximity Read ↗

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