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

doi:10.1016/j.febslet.2009.12.048

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Article

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

FEBS letters - 19 Feb 2010

Watanabe Yuya, Nakamura Yoshikazu, Ito Koichi

Abstract excerpt

The bacterial translation factor RF3 promotes translation termination by recycling the tRNA-mimicking release factors, RF1 and RF2, after mature polypeptide release. RF3 also enhances the premature peptidyl-tRNA drop-off reaction in the presence of RRF and EF-G. Despite the recently resolved X-ray crystal structure of RF3, the molecular details of the bimodal functionality of RF3 remain obscure. In this report,...

Topics

Base Sequence
Binding Sites
Escherichia coli
Escherichia coli Proteins
Models, Molecular
Mutation
Peptide Termination Factors
Protein Conformation
Protein Structure, Tertiary
RNA, Transfer, Amino Acyl
Structure-Activity Relationship

Source

Open in PubMed

Identifiers

PMID: 20043913
DOI: 10.1016/j.febslet.2009.12.048

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