Journal
CELL STRESS & CHAPERONES
Volume 17, Issue 3, Pages 361-373Publisher
SPRINGER
DOI: 10.1007/s12192-011-0312-4
Keywords
Chaperone-dependent protein disaggregation; Protein aggregation; Prion curing agent-guanidine hydrochloride; Hsp70; Hsp100
Categories
Funding
- Polish Ministry of Science and Higher Education [N301 507338]
- TEAM/2009/-3/5 program
Ask authors/readers for more resources
Besides its beneficial role in thermotolerance, the chaperone protein Hsp104 is involved in the inheritance of yeast Saccharomyces cerevisiae prions. Guanidine hydrochloride was previously shown to interfere with Hsp104 chaperone activity in vivo, thus impairing thermotolerance and resulting in prion curing. It was also reported that guanidine inhibits Hsp104 ATPase and disaggregation activity. We show that in vitro guanidine significantly inhibits the disaggregation activity of ClpB, the bacterial orthologue of Hsp104. However, guanidine exerts opposite effects on the ATPase activities of Hsp104 and ClpB. While the ATPase activity of Hsp104 is inhibited, the analogous ClpB activity is stimulated several-fold. Mutation of the universally conserved aspartic acid residue in position 184 to serine (D184S) in HSP104 and the analogous mutation in clpB (D178S) resulted in chaperones with lower disaggregating and ATPase activities. The activities of such changed chaperones are not influenced by guanidine, which suggests the role of this residue in the interaction with guanidine.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available