Protein folding has often been assumed to be a spontaneous process, a classic example of biological """"""""self-assembly"""""""". However, it has recently become apparent that protein folding and assembly of multimeric protein complexes can be catalyzed by other proteins. the highly conserved heat shock proteins (HSPs) comprise one class of these so-called """"""""chaperonins"""""""". The long term goal of the proposed research is to determine the mechanism of action of the recently discovered DnaJ family of eukaryotic heat shock protein homologues. In bacteria, DnaJ interacts with and modulates the activities of DnaK, the HSP70 cognate. The proposed experiments are designed with this paradigm in mind. A combination of yeast genetics, molecular biological, and biochemical approaches will be employed.
The specific aims are: 1) to determine the role of Scjs in protein translocation into organelles; 2) to define the interaction between Scjs and HSP70s; 3) to test the hypothesis that each eukaryotic HSP70 will have one or more like DnaJ-like partners; and 4) to dissect the proposed domain organization of Scjs.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM047385-03
Application #
2184792
Study Section
Cellular Biology and Physiology Subcommittee 1 (CBY)
Project Start
1992-05-01
Project End
1996-05-31
Budget Start
1994-06-01
Budget End
1995-05-31
Support Year
3
Fiscal Year
1994
Total Cost
Indirect Cost
Name
Dana-Farber Cancer Institute
Department
Type
DUNS #
149617367
City
Boston
State
MA
Country
United States
Zip Code
02215
Silberstein, S; Schlenstedt, G; Silver, P A et al. (1998) A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum. J Cell Biol 143:921-33