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Molecular biology

Mature proteins braced by a chaperone

Nature volume 539, pages 361–362 (2016)Cite this article

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Hsp70 chaperone molecules help other proteins to fold, and were thought to bind mainly to unfolded proteins. Single-molecule experiments now suggest that Hsp70s can also stabilize almost fully folded proteins. See Letter p.448

Cell function depends not only on the proper folding and localization of proteins when they are synthesized, but also on maintaining the well-being of fully folded (mature) proteins, and on their disposal when they are irretrievably damaged1. Seventy-kilodalton-sized heat-shock proteins (Hsp70s) are a major class of ubiquitous molecular 'chaperones' that have key roles in maintaining protein homeostasis2,3. Hsp70s interact with short stretches of amino-acid residues in extended conformations, such as those in unfolded proteins4, and thus prevent such proteins from misfolding and aggregating. But on page 448, Mashaghi et al.5 report that Hsp70s are more flexible in their binding ability than was previously appreciated: they also interact with intermediates in folding processes, and with nearly fully folded proteins. This suggests that Hsp70s play a bigger part in protein homeostasis than was thought.

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Figure 1: Different roles of Hsp70s in protein folding.

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Author notes

  1. Elizabeth A. Craig is in the Department of Biochemistry, University of Wisconsin–Madison, Madison, Wisconsin 53706-1544, USA.

Authors and Affiliations

  1. Qinglian Liu is in the Department of Physiology and Biophysics, Virginia Commonwealth University, Richmond, Virginia 23298-0551, USA.,

    Qinglian Liu & Elizabeth A. Craig

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  1. Qinglian Liu
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  2. Elizabeth A. Craig
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Correspondence to Qinglian Liu or Elizabeth A. Craig.

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Liu, Q., Craig, E. Mature proteins braced by a chaperone. Nature 539, 361–362 (2016). https://doi.org/10.1038/nature20470

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