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Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation
Open accessAbstract
Summary: 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 ibpAB Δ 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 ibpAB Δ clpB mutant cells, establishing the positions of sHsps and ClpB in this chaperone triade.
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Cited by
Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response
Wang, W., Vinocur, B., Shoseyov, O., & Altman, A. (2004) · Trends in Plant Science · doi:10.1016/j.tplants.2004.03.006 · Cited by 2,759
Recombinant protein folding and misfolding in Escherichia coli
Baneyx, F., & Mujacic, M. (2004) · Nature Biotechnology · doi:10.1038/nbt1029 · Cited by 1,445
Aphid Thermal Tolerance Is Governed by a Point Mutation in Bacterial Symbionts
Dunbar, H. E., Wilson, A. C. C., Ferguson, N. R., & Moran, N. A. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050096 · Cited by 458
Chaperones in control of protein disaggregation
Liberek, K., Lewandowska, A., & Ziętkiewicz, S. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601970 · Cited by 425
Protein quality in bacterial inclusion bodies
Ventura, S., & Villaverde, A. (2006) · Trends in Biotechnology · doi:10.1016/j.tibtech.2006.02.007 · Cited by 381
Metadata
- Authors
- Mogk, A., Deuerling, E., Vorderwülbecke, S., Vierling, E., & Bukau, B.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2003-08-27
- Volume
- 50
- Issue
- 2
- Pages
- 585-595
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2136898237
- Cited by
- 374
- References
- 0
- FWCI
- 5.79
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Mogk, A., Deuerling, E., Vorderwülbecke, S., Vierling, E., & Bukau, B. (2003). Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Molecular Microbiology. https://doi.org/10.1046/j.1365-2958.2003.03710.x
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