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Printable Handouts
Navigable Slide Index
- Introduction
- GroEL discovery: studies with bacteriophages
- The bacteriophage life-cycle
- Mutant selection in host not propagating phage
- The groE locus
- GroES and GroEL are large oligomeric proteins
- GroEL homologues
- Nomenclature
- Levels of GroEL in the cell
- Key role of GroEL in normal growth
- Defects of strains with a groELts mutation
- Chaperonins reduce protein aggregation
- DnaK/DnaJ and GroEL/GroES activity in folding
- Why do cells need chaperones?
- Which proteins does GroEL bind in the cell?
- Three types of protein
- Identification of GroEL substrates
- Confirmation of GroEL substrates (1)
- Confirmation of GroEL substrates (2)
- How many proteins interact with GroEL?
- General conclusions
- Chaperonins in other bacteria
- Chaperonins' function in other bacteria (1)
- Chaperonins' function in other bacteria (2)
- Can Cpn60 act as an adhesin?
- The enigma of multiple cpn operons
- Functional specialisation in the Rhizobia
- Functional specialisation in the Actinobacteria
- Functional specialisation in M. smegmatis (1)
- Functional specialisation in M. smegmatis (2)
- 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
Talk Citation
Lund, P. (2007, October 1). The roles of chaperonins in bacteria [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved October 16, 2024, from https://doi.org/10.69645/VYXI5908.Export Citation (RIS)
Publication History
Financial Disclosures
- Dr. Peter Lund has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.