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Distinct XPPX sequence motifs induce ribosome stalling, which is rescued by the translation elongation factor EF-P

In English

Författare

  • Lauri Peil
  • Agata L Starosta
  • Jürgen Lassak
  • Gemma C Atkinson
  • Kai Virumäe
  • Michaela Spitzer
  • Tanel Tenson
  • Kirsten Jung
  • Jaanus Remme
  • Daniel N Wilson

Summary, in English

Ribosomes are the protein synthesizing factories of the cell, polymerizing polypeptide chains from their constituent amino acids. However, distinct combinations of amino acids, such as polyproline stretches, cannot be efficiently polymerized by ribosomes, leading to translational stalling. The stalled ribosomes are rescued by the translational elongation factor P (EF-P), which by stimulating peptide-bond formation allows translation to resume. Using metabolic stable isotope labeling and mass spectrometry, we demonstrate in vivo that EF-P is important for expression of not only polyproline-containing proteins, but also for specific subsets of proteins containing diprolyl motifs (XPP/PPX). Together with a systematic in vitro and in vivo analysis, we provide a distinct hierarchy of stalling triplets, ranging from strong stallers, such as PPP, DPP, and PPN to weak stallers, such as CPP, PPR, and PPH, all of which are substrates for EF-P. These findings provide mechanistic insight into how the characteristics of the specific amino acid substrates influence the fundamentals of peptide bond formation.

Publiceringsår

2013

Språk

Engelska

Sidor

15265-15270

Publikation/Tidskrift/Serie

Proceedings of the National Academy of Sciences of the United States of America

Volym

110

Issue

38

Dokumenttyp

Artikel i tidskrift

Förlag

National Academy of Sciences

Nyckelord

  • Amino Acid Motifs/genetics
  • Chromatography, Liquid
  • Escherichia coli K12/metabolism
  • Humans
  • Peptide Elongation Factors/metabolism
  • Proline/metabolism
  • Protein Biosynthesis/physiology
  • Proteomics
  • Ribosomes/metabolism
  • Tandem Mass Spectrometry
  • beta-Galactosidase

Aktiv

Published

ISBN/ISSN/Övrigt

  • ISSN: 1091-6490