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Article

Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity.

Nature structural & molecular biology - 1 Feb 2007

Doyle Shannon M, Shorter James, Zolkiewski Michal, Hoskins Joel R, Lindquist Susan, Wickner Sue

Abstract excerpt

Two members of the AAA+ superfamily, ClpB and Hsp104, collaborate with Hsp70 and Hsp40 to rescue aggregated proteins. However, the mechanisms that elicit and underlie their protein-remodeling activities remain unclear. We report that for both Hsp104 and ClpB, mixtures of ATP and ATP-gammaS unexpectedly unleash activation, disaggregation and unfolding activities independent of cochaperones. Mutations reveal how...

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Identifiers

PMID: 17259993
DOI: 10.1038/nsmb1198
PMCID: PMC1793998

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Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity.PMID 17259993Read ↗

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