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1. Introduction
2. Molecular chaperones
3. Small heat shock proteins and alpha-crystallins
4. Number of small HSP genes in diverse species
5. Higher plant sHSPs are highly diversified
6. Mammalian, bacterial and plant sHSP evolution
7. Number of small HSP genes in diverse species
8. Biological roles of sHSPs
9. sHSP/alpha-crystallin structures (1)
10. Comparison of sHSP structures
11. sHSP monomer structure
12. Dimerization: monomer strand exchange
13. Assmebly of wheat Hsp16.9 oligomer
14. Conserved C-terminal extension contacts
15. C-terminal conserved motif in plant sHSPs
16. sHSP sub-structure and oligomer assembly
17. sHSP/alpha-crystallin structures (2)
18. Tsp36 - an sHSP from Taenia saginata
19. Alpha-crystallin domain structure in Tsp36
20. A beta-sandwich edge is patched by N-terminus
21. sHSP function and mechanism of action
22. Proposed cellular roles of small HSPs
23. Model for sHSP chaperone action
24. Analytical ultracentrifugation of wheat Hsp16.9
25. Similarity of sHSPs from different plant species
26. Rapid dimer exchange between related sHSPs
27. Subunit exchange rate of related sHSPs
28. N and C terminal extensions fully exchange
29. Dynamics of sHSP olligomerization - summary
30. Oligomeric-dimer transition
31. Model for sHSP transition to active form
32. Pea Hsp18.1 chaperone activity on MDH
33. Pea Hsp18.1 chaperone activity on luciferase
34. sHSP-substrate complex
35. Formation of sHSP-substrate (MDH) complexes
36. Detecting conformation of protected substrate
37. sHSPs stabilize MDH during heating
38. sHSP-substrate complex - conclusion
39. Role of HSP100/ClpB and chaperonins (1)
40. Role of HSP100/ClpB and chaperonins (2)
41. Model genetic system search to study sHSPs
42. Synechocystis: a model for sHSPs studies
43. Finding amino acids important for sHSPs
44. Loss of function mutations in HSP16.6 (1)
45. Loss of function mutants still produce sHSP
46. Loss of function mutations in HSP16.6 (2)
47. Ten HSP16.6 mutants - oligomeric structure
48. In vitro chaperone activity of Hsp16.6 mutants
49. Model for sHSP chaperone action - summary
50. Some remaining questions (1)
51. N-terminus exposed when sHSP dissociates
52. Some remaining questions (2)
53. Concluding remark
54. Acknowledgements
55. Useful references

Topics Covered

• Small HSP diversity and evolution
• Biological roles of sHSPs
• sHSP structure and oligomeric assembly
• Model of sHSP chaperone activity
• sHSP oligomer dynamics
• sHSP substrate interactions
• Testing sHSP function in vivo

Links

Series:

• Molecular Chaperones

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Vierling, E. (2007, October 1). Mechanism of chaperone action of small heat shock proteins [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved November 21, 2024, from https://doi.org/10.69645/UEQC2592.
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Publication History

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

Financial Disclosures

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