Quality control by the ribosome following peptide bond formation

Hani S. Zaher, Rachel Green

Research output: Contribution to journalArticle

Abstract

The overall fidelity of protein synthesis has been thought to rely on the combined accuracy of two basic processes: the aminoacylation of transfer RNAs with their cognate amino acid by the aminoacyl-tRNA synthetases, and the selection of cognate aminoacyl-tRNAs by the ribosome in cooperation with the GTPase elongation factor EF-Tu. These two processes, which together ensure the specific acceptance of a correctly charged cognate tRNA into the aminoacyl (A) site, operate before peptide bond formation. Here we report the identification of an additional mechanism that contributes to high fidelity protein synthesis after peptidyl transfer, using a well-defined in vitro bacterial translation system. In this retrospective quality control step, the incorporation of an amino acid from a non-cognate tRNA into the growing polypeptide chain leads to a general loss of specificity in the A site of the ribosome, and thus to a propagation of errors that results in abortive termination of protein synthesis.

Original languageEnglish (US)
Pages (from-to)161-166
Number of pages6
JournalNature
Volume457
Issue number7226
DOIs
StatePublished - Jan 8 2009

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Quality control by the ribosome following peptide bond formation'. Together they form a unique fingerprint.

  • Cite this