Journal
FEBS LETTERS
Volume 583, Issue 18, Pages 2991-2996Publisher
WILEY
DOI: 10.1016/j.febslet.2009.08.020
Keywords
ClpB; DnaK; Chaperone association; Protein aggregation; Aggregate reactivation
Funding
- Ministerio de Educacion y Ciencia [BFU2007-64452]
- Diputacion Foral de Bizkaia [DIPE08/18]
- Gobierno Vasco and Ministerio de Educacion y Ciencia
- Ramon y Cajal
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Intracellular protein aggregates formed under severe thermal stress can be reactivated by the concerted action of the Hsp70 system and Hsp100 chaperones. We analyzed here the interaction of DnaJ/DnaK and ClpB with protein aggregates. We show that aggregate properties modulate chaperone binding, which in turn determines aggregate reactivation efficiency. ClpB binding strictly depends on previous DnaK association with the aggregate. The affinity of ClpB for the aggregate-DnaK complex is low (K-d = 5-10 mu M), indicating a weak interaction. Therefore, formation of the DnaK - ClpB bichaperone network is a three step process. After initial DnaJ binding, the cochaperone drives association of DnaK to aggregates, and in the third step, as shown here, DnaK mediates ClpB interaction with the aggregate surface.
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