In Vivo Bipartite Interaction Between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae

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 Si...

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Hlavní autoři: Aron, Rebecca, Lopez, Nelson, Walter, William, Craig, Elizabeth A., Johnson, Jill
Médium: Článek
Jazyk:English
Vydáno: Genetics Society of America 2005
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Investigations
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1449600/
https://ncbi.nlm.nih.gov/pubmed/15687271
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1534/genetics.104.037242
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spelling pubmed-14496002006-09-13 In Vivo Bipartite Interaction Between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae Aron, Rebecca Lopez, Nelson Walter, William Craig, Elizabeth A. Johnson, Jill Genetics Investigations 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 Sis1ΔG/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 Sis1ΔG/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 Sis1ΔG/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. Genetics Society of America 2005-04 /pmc/articles/PMC1449600/ /pubmed/15687271 http://dx.doi.org/10.1534/genetics.104.037242 Text en Copyright © 2005, Genetics Society of America
institution US National Library of Medicine
collection PubMed Central
language English
format Article
topic Investigations
spellingShingle Investigations
Aron, Rebecca
Lopez, Nelson
Walter, William
Craig, Elizabeth A.
Johnson, Jill
In Vivo Bipartite Interaction Between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae
description 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 Sis1ΔG/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 Sis1ΔG/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 Sis1ΔG/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.
author Aron, Rebecca
Lopez, Nelson
Walter, William
Craig, Elizabeth A.
Johnson, Jill
author_facet Aron, Rebecca
Lopez, Nelson
Walter, William
Craig, Elizabeth A.
Johnson, Jill
author_sort Aron, Rebecca
title In Vivo Bipartite Interaction Between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae
title_short In Vivo Bipartite Interaction Between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae
title_full In Vivo Bipartite Interaction Between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae
title_fullStr In Vivo Bipartite Interaction Between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae
title_full_unstemmed In Vivo Bipartite Interaction Between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae
title_sort in vivo bipartite interaction between the hsp40 sis1 and hsp70 in saccharomyces cerevisiae
publisher Genetics Society of America
publisher_facet Genetics Society of America
publishDate 2005
url https://ncbi.nlm.nih.gov/pmc/articles/PMC1449600/
https://ncbi.nlm.nih.gov/pubmed/15687271
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1534/genetics.104.037242
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