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Article

A model for how ribosomal release factors induce peptidyl-tRNA cleavage in termination of protein synthesis.

Molecular cell - 7 Sept 2007

Trobro Stefan, Aqvist Johan

Abstract excerpt

A major unresolved question in messenger RNA translation is how ribosomal release factors terminate protein synthesis. Class 1 release factors decode stop codons and trigger hydrolysis of the bond between the nascent polypeptide and tRNA some 75 A away from the decoding site. While the gross features of the release factor-ribosome interaction have been revealed by low-resolution crystal structures, there is no...

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PMID: 17803940
DOI: 10.1016/j.molcel.2007.06.032

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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A model for how ribosomal release factors induce peptidyl-tRNA cleavage in termination of protein synthesis.PMID 17803940Read ↗

Peptide release on the ribosome: mechanism and implications for translational control.Semantic proximity Read ↗

Two distinct conformations of the conserved RNA-rich decoding center of the small ribosomal subunit are recognized by tRNAs and release factors.Semantic proximity Read ↗

Stop codon recognition by release factors induces structural rearrangement of the ribosomal decoding center that is productive for peptide release.Semantic proximity Read ↗

The critical role of the universally conserved A2602 of 23S ribosomal RNA in the release of the nascent peptide during translation termination.Semantic proximity Read ↗

Mutations at the accommodation gate of the ribosome impair RF2-dependent translation termination.Semantic proximity Read ↗

Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3.Semantic proximity Read ↗

Mutations in conserved regions of ribosomal RNAs decrease the productive association of peptide-chain release factors with the ribosome during translation termination.Semantic proximity Read ↗

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.Semantic proximity Read ↗

The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release.Semantic proximity Read ↗

R213I mutation in release factor 2 (RF2) is one step forward for engineering an omnipotent release factor in bacteria Escherichia coli.Semantic proximity Read ↗

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

Thermodynamic and kinetic insights into stop codon recognition by release factor 1.Semantic proximity Read ↗

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