• Overview of Molecular Chaperones
• 34 min
  1. History of the molecular chaperone concept: roles in assembly processes

  • Prof. Emeritus R. John Ellis
• 34 min
  2. Chaperone mechanisms in cellular protein folding

  • Prof. Dr. F. Ulrich Hartl
• Prokaryotic Molecular Chaperones
• 38 min
  3. Mechanistic aspects of chaperonin GroEL/ES function

  • Prof. Amnon Horovitz
• 99 min
  4. Structure and function of the ATP-dependent Clp chaperone/protease machines

  • Dr. Michael R. Maurizi
• 32 min
  5. The role of chaperones and Sec machinery in protein secretion

  • Prof. Koreaki Ito
• 44 min
  6. How can molecular chaperones repair damaged protein structures?

  • Prof. Pierre Goloubinoff
• 32 min
  7. Disulfide bond formation in vivo

  • Prof. James Bardwell
• Eukaryotic Molecular Chaperones
• 39 min
  8. Overview of eukaryotic molecular chaperones in the cytosol

  • Dr. Jason C. Young
• 36 min
  9. Chaperonin-containing TCP-1 (CCT), actin springs, and protein folding fluxes

  • Prof. Keith Willison
• 35 min
  10. The functions of the Hsp70 system

  • Prof. Jeffrey L. Brodsky
• 26 min
  11. Hsp90: a chaperone for protein kinases and hormone receptors

  • Dr. David Toft
• Role of Chaperones in Diseases
• 38 min
  12. The roles of molecular chaperones in bacterial infection

  • Prof. Tomoko Yamamoto
• 46 min
  13. Role of chaperonin-like proteins in Bardet-Biedl syndrome

  • Dr. Michel R. Leroux
• 53 min
  14. Roles for molecular chaperones in cystic fibrosis

  • Prof. Douglas M. Cyr
• 51 min
  15. Targeting cancer: designing drugs against Hsp90

  • Dr. Gabriela Chiosis
• Archived Lectures *These may not cover the latest advances in the field
• 29 min
  16. Overview of prokaryotic molecular chaperones

  • Prof. Walid A. Houry
• 47 min
  17. The biogenesis of E. coli inner membrane proteins

  • Dr. Joen Luirink
• 39 min
  18. Mechanism of chaperone action of small heat shock proteins

  • Prof. Elizabeth Vierling
• 22 min
  19. ClpB: a chaperone for protein disaggregation

  • Prof. Michal Zolkiewski
• 38 min
  20. The roles of chaperonins in bacteria

  • Dr. Peter Lund
• 44 min
  21. Towards a unifying mechanism for the Hsp70 chaperones

  • Prof. Pierre Goloubinoff
• 29 min
  22. Adaptor mediated activation of the Hsp100/ Clp protein ClpC controls general and regulatory proteolysis in Bacillus subtilis

  • Prof. Dr. Kursad Turgay
• 33 min
  23. Hsp31: a general stress protein of Escherichia coli

  • Prof. Francois Baneyx
• 46 min
  24. Hsp104: a specialized chaperone for protein disaggregation

  • Dr. John R. Glover
• 47 min
  25. Molecular chaperones and handling of abnormal proteins in neurodegenerative disorders

  • Prof. Michael Sherman
• 20 min
  26. The role of chaperones in Parkinson's disease

  • Dr. Konstanze F. Winklhofer

Printable Handouts

PDF

Navigable Slide Index

1. Introduction
2. GroEL discovery: studies with bacteriophages
3. The bacteriophage life-cycle
4. Mutant selection in host not propagating phage
5. The groE locus
6. GroES and GroEL are large oligomeric proteins
7. GroEL homologues
8. Nomenclature
9. Levels of GroEL in the cell
10. Key role of GroEL in normal growth
11. Defects of strains with a groELts mutation
12. Chaperonins reduce protein aggregation
13. DnaK/DnaJ and GroEL/GroES activity in folding
14. Why do cells need chaperones?
15. Which proteins does GroEL bind in the cell?
16. Three types of protein
17. Identification of GroEL substrates
18. Confirmation of GroEL substrates (1)
19. Confirmation of GroEL substrates (2)
20. How many proteins interact with GroEL?
21. General conclusions
22. Chaperonins in other bacteria
23. Chaperonins' function in other bacteria (1)
24. Chaperonins' function in other bacteria (2)
25. Can Cpn60 act as an adhesin?
26. The enigma of multiple cpn operons
27. Functional specialisation in the Rhizobia
28. Functional specialisation in the Actinobacteria
29. Functional specialisation in M. smegmatis (1)
30. Functional specialisation in M. smegmatis (2)
31. Final conclusions

Topics Covered

• The discovery of the GroEL chaperonin in E. coli
• Organization of the GroEL and GroES genes
• Oligomeric structure of GroEL and GroES proteins
• Key roles of GroEL
• The substrates of GroEL
• Chaperonins in other bacteria and their roles

Links

Series:

• Molecular Chaperones

Categories:

• Biochemistry
• Cell Biology
• Microbiology

Talk Citation

Publication History

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

Financial Disclosures

• Dr. Peter Lund has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.