DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface

• Published in: FEBS letters Vol. 583; no. 18; pp. 2991 - 2996
• Main Authors: Acebrón, Sergio P., Martín, Ianire, del Castillo, Urko, Moro, Fernando, Muga, Arturo
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 17.09.2009
• Subjects: Aggregate reactivation; Chaperone association; ClpB; DnaK; Endopeptidase Clp; Escherichia coli Proteins - metabolism; Heat-Shock Proteins - metabolism; HSP40 Heat-Shock Proteins; HSP70 Heat-Shock Proteins - metabolism; Molecular Chaperones - metabolism; Protein aggregation; Protein Binding; Protein aggregation; ClpB; DnaK; Chaperone association; Aggregate reactivation
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2009.08.020

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 μM), 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. MINT- 7258957: G6PDH (uniprotkb: P0AC53) and G6PDH (uniprotkb: P0AC53) bind (MI: 0407) by dynamic light scattering (MI: 0038)MINT- 7258951: alpha glucosidase (uniprotkb: P21517) and alpha glucosidase (uniprotkb: P21517) bind (MI: 0407) by dynamic light scattering (MI: 0038) MINT- 7258903: AdhE (uniprotkb: P0A9Q7) and AdhE (uniprotkb: P0A9Q7) bind (MI: 0407) by dynamic light scattering (MI: 0038) MINT- 7258900: G6PDH (uniprotkb: P0AC53) and G6PDH (uniprotkb: P0AC53) bind (MI: 0407) by biophysical (MI: 0013) MINT- 7258974: DnaK (uniprotkb: P0A6Y8), ClpB (uniprotkb: P63284), DnaJ (uniprotkb: P08622) and G6PDH (uniprotkb: P0AC53) physically interact (MI: 0914) by cosedimentation (MI: 0027)