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The essential role of the invariant GGQ motif in the function and stability <i>in vivo</i> of bacterial release factors RF1 and RF2

18 Dec 2002

Abstract excerpt

Release factors RF1 and RF2 are required in bacteria for the cleavage of peptidyl-tRNA. A single sequence motif, GGQ, is conserved in all eubacterial, archaebacterial and eukaryotic release factors and may mimic the CCA end of tRNA, although the position of the motif in the crystal structures of human eRF1 and Escherichia coli RF2 is strikingly different. Mutations have been introduced at each of the three...

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PMID: 12492870
DOI: 10.1046/j.1365-2958.2003.03301.x

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Related research

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The essential role of the invariant GGQ motif in the function and stability <i>in vivo</i> of bacterial release factors RF1 and RF2PMID 12492870Read ↗

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

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Eukaryotic release factor 3 is required for multiple turnovers of peptide release catalysis by eukaryotic release factor 1.Semantic proximity Read ↗

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

Deficiency in a glutamine-specific methyltransferase for release factor causes mouse embryonic lethality.Semantic proximity Read ↗

[Mutation of a glutamine residue in the universal tripeptide GGQ in human eRF1 termination factor does not cause complete loss of its activity].Semantic proximity Read ↗

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