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. 2010 Dec;6(12):914-20.
doi: 10.1038/nchembio.455. Epub 2010 Oct 17.

The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase

Sandeep K Sharma  1 , Paolo De los Rios, Philipp Christen, Ariel Lustig, Pierre Goloubinoff
Affiliations

The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase

Sandeep K Sharma et al. Nat Chem Biol. 2010 Dec.

Abstract

Hsp70-Hsp40-NEF and possibly Hsp100 are the only known molecular chaperones that can use the energy of ATP to convert stably pre-aggregated polypeptides into natively refolded proteins. However, the kinetic parameters and ATP costs have remained elusive because refolding reactions have only been successful with a molar excess of chaperones over their polypeptide substrates. Here we describe a stable, misfolded luciferase species that can be efficiently renatured by substoichiometric amounts of bacterial Hsp70-Hsp40-NEF. The reactivation rates increased with substrate concentration and followed saturation kinetics, thus allowing the determination of apparent V(max)' and K(m)' values for a chaperone-mediated renaturation reaction for the first time. Under the in vitro conditions used, one Hsp70 molecule consumed five ATPs to effectively unfold a single misfolded protein into an intermediate that, upon chaperone dissociation, spontaneously refolded to the native state, a process with an ATP cost a thousand times lower than expected for protein degradation and resynthesis.

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Comment in

  • Chaperones: A story of thrift unfolds.
    Baneyx F, Nannenga BL. Baneyx F, et al. Nat Chem Biol. 2010 Dec;6(12):880-1. doi: 10.1038/nchembio.468. Nat Chem Biol. 2010. PMID: 21079597 No abstract available.

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