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Originally published as Genetics Published Articles Ahead of Print on January 31, 2005.
Genetics, Vol. 169, 1873-1882, April 2005, Copyright © 2005
doi:10.1534/genetics.104.037242
In Vivo Bipartite Interaction Between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae
Rebecca Aron*,
,1,
Nelson Lopez*,
,1,2,
William Walter*,
Elizabeth A. Craig*,3 and
Jill Johnson*,4
* Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706
Graduate Program in Biomolecular Chemistry, University of Wisconsin, Madison, Wisconsin 53706
Graduate Program in Bacteriology, University of Wisconsin, Madison, Wisconsin 53706
3 Corresponding author: Department of Biochemistry, 441E Biochemistry Addition, 433 Babcock Dr., University of Wisconsin, Madison, WI 53706.
E-mail: ecraig{at}wisc.edu
The essential Hsp40, Sis1, is a J-protein cochaperone for the Ssa class of Hsp70's of Saccharomyces cerevisiae. Sis1 is required for the maintenance of the prion [RNQ+], as Sis1 lacking its 55-amino-acid glycine-rich region (G/F) does not maintain [RNQ+]. We report that overexpression of Sis1
G/F in an otherwise wild-type strain had a negative effect on both cell growth and [RNQ+] maintenance, while overexpression of wild-type Sis1 did not. Overexpression of the related Hsp40 Ydj1 lacking its G/F region did not cause inhibition of growth, indicating that this dominant effect of Sis1G/F is not a characteristic shared by all Hsp40's. Analysis of small deletions within the SIS1 G/F region indicated that the observed dominant effects were caused by the absence of sequences known to be important for Sis1's unique cellular functions. These inhibitory effects of Sis1G/F were obviated by alterations in the N-terminal J-domain of Sis1 that affect interaction with Ssa's ATPase domain. In addition, a genetic screen designed to isolate additional mutations that relieved these inhibitory effects identified two residues in Sis1's carboxy-terminal domain. These alterations disrupted the interaction of Sis1 with the 10-kD carboxy-terminal regulatory domain of Ssa1, indicating that Sis1 has a bipartite interaction with Ssa in vivo.
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