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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.