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- Title
Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation.
- Authors
Mogk, Axel; Deuerling, Elke; Vorderwülbecke, Sonja; Vierling, Elizabeth; Bukaui, Bernd
- Abstract
Small heat shock proteins (sHsps) can efficiently prevent the aggregation of unfolded proteins in vitro. However, how this in vitro activity translates to function in vivo is poorly understood. We demonstrate that sHsps of Escherichia coli, IbpA and IbpB, co-operate with ClpB and the DnaK system in vitro and in vivo, forming a functional triade of chaperones. IbpA/IbpB and ClpB support independently and co-operatively the DnaK system in reversing protein aggregation. A Δ ibpABΔ clpB double mutant exhibits strongly increased protein aggregation at 42°C compared with the single mutants. sHsp and ClpB function become essential for cell viability at 37°C if DnaK levels are reduced. The DnaK requirement for growth is increasingly higher for Δ ibpAB, Δ clpB, and the double Δ ibpABΔ clpB mutant cells, establishing the positions of sHsps and ClpB in this chaperone triade.
- Subjects
ESCHERICHIA coli; HEAT shock proteins; MOLECULAR chaperones; PROTEINS; GENETIC mutation
- Publication
Molecular Microbiology, 2003, Vol 50, Issue 2, p585
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1046/j.1365-2958.2003.03710.x