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Chaperones

A story of thrift unfolds

Nature Chemical Biology volume 6, pages 880–881 (2010)Cite this article

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Although members of the Hsp70-DnaK family of heat shock proteins are involved in nearly all aspects of cell physiology, some mechanistic details of their mode of action remain obscure. A new substrate helps establish DnaK as an unfoldase that requires as little as five ATP molecules to drive the refolding of one protein.

Globular proteins are flexible macromolecules that have evolved to perform optimally within the context of a well-defined cellular environment. It is therefore not surprising that heat shock and other forms of stress affecting the physico-chemical properties of the cellular milieu trigger local or global unfolding events that ultimately lead to protein aggregation or degradation. Aside from dedicated systems responsible for the maintenance of cellular homeostasis, the universally conserved molecular chaperones are the principal line of defense used by living systems to mitigate the deleterious effects of stress. In addition to stabilizing and refolding misfolded and aggregated proteins, molecular chaperones unfold proteins for efficient proteolysis, help nascent polypeptides reach a correct conformation, support protein translocation across membranes, assist in the assembly and disassembly of oligomeric structures and regulate the stability and activity of certain native proteins1,2,3.

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Figure 1: DnaK structure and unfoldase function.

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  1. François Baneyx and Brent L. Nannenga are in the Department of Chemical Engineering, University of Washington, Seattle.,

    François Baneyx & Brent L Nannenga

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  1. François Baneyx
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  2. Brent L Nannenga
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Correspondence to Brent L Nannenga.

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Baneyx, F., Nannenga, B. A story of thrift unfolds. Nat Chem Biol 6, 880–881 (2010). https://doi.org/10.1038/nchembio.468

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