The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Unraveling the Mechanism of Protein Disaggregation Through a ClpB-DnaK Interaction
Abstract
Dissecting Disaggregation: The excessive accumulation of misfolded protein aggregates can overwhelm the cell's "quality control" machinery, leading to cell death. The yeast Hsp104 protein and its bacterial homolog ClpB are molecular chaperones that can "rescue" aggregated proteins by coupling the force generated from adenosine triphosphate hydrolysis to the progressive unfolding and threading of extended polypeptide segments through axial channels in these large molecular machines. Unfolded polypeptides emerging from the channel are refolded with the aid of a second chaperone system, DnaK/DnaJ/GrpE. DnaK also plays an important role in bringing regions of polypeptides within aggregates to ClpB to begin the solubilization process. Rosenzweig et al. (p. 1080 , published online 7 February; see the Perspective by Saibil ) describe a nuclear magnetic resonance–derived structure of the ClpB-DnaK complex, and verified it through mutagenesis and functional assays. The work clarifies the roles of each of the molecular players in the disaggregation reaction and provides a structural basis for the DnaK-ClpB interaction.
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Citations
Cites
HADDOCK: A Protein−Protein Docking Approach Based on Biochemical or Biophysical Information
Dominguez, C., Boelens, R., & Bonvin, A. M. J. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja026939x · Cited by 3,187
Garcı́a de la Torre, J., Huertas, M. L., & Carrasco, B. (2000) · Journal of Magnetic Resonance · doi:10.1006/jmre.2000.2170 · Cited by 551
Cited by
Rosenzweig, R., Nillegoda, N. B., Mayer, M. P., & Bukau, B. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0133-3 · Cited by 1,285
Self-citationRecent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones
Mayer, M. P., & Gierasch, L. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.002810 · Cited by 295
Structural basis for protein antiaggregation activity of the trigger factor chaperone.
Saio, T., Guan, X., Rossi, P., Economou, A., & Kalodimos, C. G. (2014) · Science · doi:10.1126/science.1250494 · Cited by 289
Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling
Genest, O., Hoskins, J. R., Kravats, A. N., Doyle, S. M., & Wickner, S. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.10.010 · Cited by 76
Chaperone-Bound Clients: The Importance of Being Dynamic
Hiller, S. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.12.005 · Cited by 54
Metadata
- Authors
- Rosenzweig, R., Moradi, S., Zarrine-Afsar, A., Glover, J. R., & Kay, L. E.
- Venue
- Science
- Published
- 2013-03
- Volume
- 339
- Issue
- 6123
- Pages
- 1080-1083
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2117195560
- Cited by
- 260
- References
- 2
- FWCI
- 12.78
- Type
- journal article
- Language
- en
- Open access
- closed
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