Printable Handouts

PDF

Navigable Slide Index

1. Introduction
2. Protein folding and misfolding
3. Protein disaggregation in yeast
4. Aggregate reactivation by ClpB
5. Substrates of ClpB in vivo
6. Heat-shocked E. coli survival depends on ClpB
7. ClpB and other Clp ATPases
8. ClpB is an AAA+ ATPase
9. Domain structure of Clp ATPases
10. Structure of ClpB monomer
11. Oligomeric rings of ClpB
12. Structure of hexameric ClpB
13. A ClpA-like ClpB variant degrades proteins
14. Model of protein disaggregation
15. Images of ClpB bound to aggregates
16. Peptides interacting with ClpB
17. The ClpB channel entrance
18. N-terminal domain and substrate binding
19. Dual translation initiation site in ClpB
20. Two isoforms of ClpB
21. Two isoforms cooperate in vivo
22. Motions of domains in oligomeric ClpB
23. Mutations of the middle domain of ClpB
24. Conformations of the middle domain of ClpB
25. ClpB as an ATP-driven machine
26. Binding of ClpB and DnaK
27. Reactivation depends on incubation with DnaK
28. Deceleration of ClpB ATPase enhances activity
29. Open questions
30. Acknowledgments

Topics Covered

• ClpB, a AAA+ ATPase capable of reactivating aggregated proteins
• ATP-dependent translocation of aggregated substrates through a channel in the oligomeric ClpB
• Role of the N-terminal domain of ClpB in substrate binding
• Role of the DnaK system of co-chaperones in the ClpB-mediated aggregate reactivation
• Mechanisms of substrate recognition by ClpB

Links

Series:

• Molecular Chaperones

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Zolkiewski, M. (2007, October 1). ClpB: a chaperone for protein disaggregation [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved November 21, 2024, from https://doi.org/10.69645/GMJB9992.
Export Citation (RIS)

Publication History

• Published on October 1, 2007
• Archived on August 13, 2020

Financial Disclosures

• Prof. Michal Zolkiewski has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.