Journal
EMBO JOURNAL
Volume 29, Issue 9, Pages 1552-1564Publisher
WILEY
DOI: 10.1038/emboj.2010.52
Keywords
chaperonin; GroEL; metabolomics; protein folding; proteomics
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Funding
- MEXT [19037007, 19058002]
- Yamagata Prefecture and Tsuruoka City
- Japan Society for the Promotion of Science
- Grants-in-Aid for Scientific Research [19058002, 19037007, 21310129] Funding Source: KAKEN
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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 similar to 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, similar to 70% of the Class IV substrates appear to be metabolic enzymes, supporting a hypothetical role of GroE in enzyme evolution. The EMBO Journal (2010) 29, 1552-1564. doi:10.1038/emboj.2010.52; Published online 1 April 2010
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