Protein Folding in vivo
Required reading:
Lodish 50-78
Landry's
Web page "Protein Interactions and Molecular Chaperones"
DebBurman, Raymond, Caughey, Lindquist (1997) "Chaperone-supervised
conversion of prion protein to its protease-resistant form"
Sample questions for the exam:
-
What treatments were used by DebBurman et al. in order to affect the protein-protein
interactions of PrPC and PrPSc?
-
Some chaperones promoted conversion of PrPC to PrP-res, but others did
not. What feature(s) distinguish them and might account for the difference
in activity?
-
Suggest a mechanism by which GroES inhibits GroEL-dependent formation of
PrP-res. Account for the fact that GroES does not inhibit GroEL-dependent
formation of PrP-res when the PrPSc is pratially denatured.
Additional reading on chaperones and evolution:
Rutherford and Lindquist (1998) "Hsp90
as a capacitor for morphological evolution"
News
and Views for above
Critical
comment by Dickinson and Seger
Lindquist
response
True and Lindquist (2000) "A
yeast prion provides a mechanism for genetic variation and phenotypic diversity"