• 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. Bacterial pathways of protein secretion
3. Protein translocation across membranes
4. Major questions in protein translocation
5. "Signal hypothesis"
6. Essential requirements for protein translocation
7. Topogenic signal sequences
8. Factors for targeting, anti-folding and unfolding
9. Trigger factor - ribosome-associated chaperone
10. Bacterial SRP system
11. SecB is an export-specific chaperone
12. Identification of Sec factors by "forward genetics"
13. Biochemical approaches for Sec factors study
14. SecYEG homologs in higher organisms
15. SecY protein
16. SecY interacts with SecE and SecG
17. Structure of archaeal SecYE-beta translocon
18. Preprotein threads through the narrow channel
19. Gating devices of the translocon
20. Role of the lateral gate of the translocon
21. Two modes of translocon use
22. YidC-SecYEG cooperation
23. Higher order assemblies of SecYEG
24. SecYEG dimerization upon ribosome binding
25. SecYEG functions as a dimer
26. SecA is an ATPase
27. SecA protomer
28. What is the working form of SecA structure?
29. SecA insertion model
30. Two modes of SecY-SecA interactions
31. SecA ATPase as a power-controllable engine
32. SecM controls SecA at different levels
33. Translation of secM is subject to "arrest"
34. SecM contains an "arrest sequence"
35. SecM is required for expression of SecA
36. "Cis-chaperone" function of SecM
37. New concepts that SecM brought to us
38. Concluding remarks

Topics Covered

• Importance of protein translocation
• Identification of Sec factors
• Structure and function of translocon, an evolutionarily conserved membrane protein complex that serves as a polypeptide-conducting channel
• Structure and function of SecA, a translocation-driving ATPase
• Unique regulation of SecA by SecM, a protein that interacts with the ribosomal exit tunnel

Links

Series:

• Molecular Chaperones

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Publication History

• Published on October 1, 2007
• Archived on May 28, 2025

Financial Disclosures

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