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1. Introduction
2. It's tough to be enteric
3. Molecular chaperones of E. coli
4. Hsp31 is conserved in some human pathogens
5. Hsp31 is an ATP-regulated chaperone
6. Hsp31 structure (1)
7. Homology of Hsp31 and P. horikoshii protease I
8. The Hsp31 family
9. Hsp31 structure (2)
10. Importance of linker-loop-shielded residues
11. The linker-loop region acts as a thermal gate
12. hchA knock-out mutants under severe heat stress
13. Hsp31 and severe heat stress management
14. Hsp31 substrates
15. hchA regulation
16. A new mechanism for heat-shock induction
17. hchA is induced by oxidative and acid stresses
18. hchA is induced by multiple stress conditions
19. Role of Hsp31 in oxidative stress management
20. Role of Hsp31 in stationary phase acid resistance
21. Protective networks
22. Acknowledgments

Topics Covered

• Stress proteins and molecular chaperones in E. coli
• Hsp31: an ATP-regulated molecular chaperone
• Hsp31 structure
• Hsp31 mechanism of action
• Role in the management of severe thermal stress
• Regulation and mechanism of thermal induction
• Induction by other stressors
• Role in the management of acid stress

Links

Series:

• Molecular Chaperones

Categories:

• Biochemistry
• Cell Biology
• Microbiology

Talk Citation

Baneyx, F. (2007, October 1). Hsp31: a general stress protein of Escherichia coli [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved April 15, 2025, from https://doi.org/10.69645/NHJY2937.
Export Citation (RIS)

Publication History

• Published on October 1, 2007
• Archived on February 25, 2021

Financial Disclosures

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