Proteomic analysis of ribosomes: Translational control of mRNA populations by glycogen synthase GYS1

Gabriele Fuchs, Camille Diges, Lori A. Kohlstaedt, Karen A. Wehner, Peter Sarnow

Research output: Contribution to journalArticlepeer-review

Abstract

Ribosomes exist as a heterogenous pool of macromolecular complexes composed of ribosomal RNA molecules, ribosomal proteins, and numerous associated "nonribosomal" proteins. To identify nonribosomal proteins that may modulate ribosome activity, we examined the composition of translationally active and inactive ribosomes using a proteomic multidimensional protein identification technology. Notably, the phosphorylated isoform of glycogen synthase, glycogen synthase 1 (GYS1), was preferentially associated with elongating ribosomes. Depletion of GYS1 affected the translation of a subset of cellular mRNAs, some of which encode proteins that modulate protein biosynthesis. These findings argue that GYS1 abundance, by virtue of its ribosomal association, provides a feedback loop between the energy state of the cells and the translation machinery.

Original languageEnglish (US)
Pages (from-to)118-130
Number of pages13
JournalJournal of molecular biology
Volume410
Issue number1
DOIs
StatePublished - Jul 1 2011

Keywords

  • energy metabolism
  • mass spectrometry
  • ribosome filter
  • translational control
  • translational profiling

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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