A systematic survey of in vivo obligate chaperonin-dependent substrates

Kei Fujiwara, Yasushi Ishihama, Kenji Nakahigashi, Tomoyoshi Soga, Hideki Taguchi

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111 Citations (Scopus)

Abstract

Chaperonins are absolutely required for the folding of a subset of proteins in the cell. An earlier proteome-wide analysis of Escherichia coli chaperonin GroEL/GroES (GroE) interactors predicted obligate chaperonin substrates, which were termed Class III substrates. However, the requirement of chaperonins for in vivo folding has not been fully examined. Here, we comprehensively assessed the chaperonin requirement using a conditional GroE expression strain, and concluded that only 60% of Class III substrates are bona fide obligate GroE substrates in vivo. The in vivo obligate substrates, combined with the newly identified obligate substrates, were termed Class IV substrates. Class IV substrates are restricted to proteins with molecular weights that could be encapsulated in the chaperonin cavity, are enriched in alanine/glycine residues, and have a strong structural preference for aggregation-prone folds. Notably, 70% of the Class IV substrates appear to be metabolic enzymes, supporting a hypothetical role of GroE in enzyme evolution.

Original languageEnglish
Pages (from-to)1552-1564
Number of pages13
JournalEMBO Journal
Volume29
Issue number9
DOIs
Publication statusPublished - 2010 May 1

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Keywords

  • Chaperonin
  • GroEL
  • Metabolomics
  • Protein folding
  • Proteomics

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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