Uniformity of Peptide Release Is Maintained by Methylation of Release Factors

William E. Pierson, Eric D. Hoffer, Hannah E. Keedy, Carrie L. Simms, Christine M. Dunham, Hani S. Zaher

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

Termination of protein synthesis on the ribosome is catalyzed by release factors (RFs), which share a conserved glycine-glycine-glutamine (GGQ) motif. The glutamine residue is methylated in vivo, but a mechanistic understanding of its contribution to hydrolysis is lacking. Here, we show that the modification, apart from increasing the overall rate of termination on all dipeptides, substantially increases the rate of peptide release on a subset of amino acids. In the presence of unmethylated RFs, we measure rates of hydrolysis that are exceptionally slow on proline and glycine residues and approximately two orders of magnitude faster in the presence of the methylated factors. Structures of 70S ribosomes bound to methylated RF1 and RF2 reveal that the glutamine side-chain methylation packs against 23S rRNA nucleotide 2451, stabilizing the GGQ motif and placing the side-chain amide of the glutamine toward tRNA. These data provide a framework for understanding how release factor modifications impact termination.

Original languageEnglish
Pages (from-to)11-18
Number of pages8
JournalCell Reports
Volume17
Issue number1
DOIs
StatePublished - Sep 27 2016

Keywords

  • methylation
  • peptide release
  • release factor
  • ribosome
  • termination
  • translation

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