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- Overview of Molecular Chaperones
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1. History of the molecular chaperone concept: roles in assembly processes
- Prof. Emeritus R. John Ellis
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2. Chaperone mechanisms in cellular protein folding
- Prof. Dr. F. Ulrich Hartl
- Prokaryotic Molecular Chaperones
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3. Mechanistic aspects of chaperonin GroEL/ES function
- Prof. Amnon Horovitz
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4. Structure and function of the ATP-dependent Clp chaperone/protease machines
- Dr. Michael R. Maurizi
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5. The role of chaperones and Sec machinery in protein secretion
- Prof. Koreaki Ito
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6. How can molecular chaperones repair damaged protein structures?
- Prof. Pierre Goloubinoff
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7. Disulfide bond formation in vivo
- Prof. James Bardwell
- Eukaryotic Molecular Chaperones
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8. Overview of eukaryotic molecular chaperones in the cytosol
- Dr. Jason C. Young
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9. Chaperonin-containing TCP-1 (CCT), actin springs, and protein folding fluxes
- Prof. Keith Willison
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10. The functions of the Hsp70 system
- Prof. Jeffrey L. Brodsky
- Role of Chaperones in Diseases
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12. The roles of molecular chaperones in bacterial infection
- Prof. Tomoko Yamamoto
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13. Role of chaperonin-like proteins in Bardet-Biedl syndrome
- Dr. Michel R. Leroux
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14. Roles for molecular chaperones in cystic fibrosis
- Prof. Douglas M. Cyr
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15. Targeting cancer: designing drugs against Hsp90
- Dr. Gabriela Chiosis
- Archived Lectures *These may not cover the latest advances in the field
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16. Overview of prokaryotic molecular chaperones
- Prof. Walid A. Houry
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17. The biogenesis of E. coli inner membrane proteins
- Dr. Joen Luirink
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18. Mechanism of chaperone action of small heat shock proteins
- Prof. Elizabeth Vierling
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19. ClpB: a chaperone for protein disaggregation
- Prof. Michal Zolkiewski
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20. The roles of chaperonins in bacteria
- Dr. Peter Lund
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21. Towards a unifying mechanism for the Hsp70 chaperones
- Prof. Pierre Goloubinoff
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23. Hsp31: a general stress protein of Escherichia coli
- Prof. Francois Baneyx
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24. Hsp104: a specialized chaperone for protein disaggregation
- Dr. John R. Glover
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26. The role of chaperones in Parkinson's disease
- Dr. Konstanze F. Winklhofer
Printable Handouts
Navigable Slide Index
- Introduction
- The protein folding process
- The cytoplasm is very crowded and viscous
- Proteins are not very stable
- Concept of a molecular chaperone
- Chaperones in E. coli
- Chaperones to be discussed
- Chaperones and biosynthesis in E. coli
- Trigger factor
- Structure of E. coli trigger factor
- Structure of E. coli TF bound to ribosome
- The cradle model of TF function
- The dynamic cycling model for TF function
- The Hsp70/Hsp40 chaperone system
- E. coli DnaK/DnaJ/GrpE structures
- DnaK/DnaJ/GrpE functional cycle
- Evidence for the K/J/E cycle from structural data
- Motifs bound by DnaK and DnaJ
- GroEL/GroES system
- GroEL/GroES structure before and after binding
- GroEL apical domain is implicated in binding
- Mechanism used by GroEL in protein binding
- GroEL cycle
- GroEL function in vivo
- The Clp ATPases
- ClpB as a protein disaggregation machine
- ClpXP complex model structure
- Substrates of ClpXP
- SsrA targets unfinished proteins for proteolysis
- ClpXP mechanism of function
- Model for substrate entry and product release
- Conclusion
Topics Covered
- Protein folding in vitro versus in vivo
- Concept of a molecular chaperone
- Chaperones in E. coli
- Trigger factor
- DnaK/DnaJ/GrpE system
- GroEL/GroES system
- Clp ATPases
Talk Citation
Houry, W.A. (2007, October 1). Overview of prokaryotic molecular chaperones [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved April 1, 2025, from https://doi.org/10.69645/VEAP7210.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Walid A. Houry has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.