Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1999-1-28
pubmed:abstractText
The Ssa subfamily of Hsp70 molecular chaperones in the budding yeast Saccharomyces cerevisiae has four members, encoded by SSA1, SSA2, SSA3, and SSA4. Deletion of the two constitutively expressed genes, SSA1 and SSA2, results in cells which are slow growing and temperature sensitive. In this study, we demonstrate that an extragenic suppressor of the temperature sensitivity of ssa1 ssa2 strains, EXA1-1, is a loss-of-function mutation in SIN1/SPT2, which encodes a nonhistone component of chromatin. Loss of function of Sin1p leads to overexpression of SSA3 in the ssa1 ssa2 mutant background, at a level which is sufficient to mediate suppression. In a strain which is wild type for SSA genes, we detected no effect of Sin1p on Ssa3p expression except under conditions of heat shock. Existing data indicate that expression of SSA3 in the ssa1 ssa2 mutant background as well as in heat-shocked wild-type strains is mediated by the heat shock transcription factor HSF. Our findings suggest that it is HSF-mediated induction of SSA3 which is modulated by Sin1p. The EXA1-1 suppressor mutation thus improves the growth of ssa1 ssa2 strains by selectively increasing HSF-mediated expression of SSA3.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-1459453, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-1473150, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-1519755, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-1644272, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-1695149, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-1729605, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-1869583, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-2004420, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-2072912, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-2121731, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-2181281, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-2188113, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-2190191, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-2527744, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-2651414, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-2674681, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-2991744, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-3037338, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-3282178, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-3282179, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-3302682, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-3333305, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-3545494, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-6329902, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-6354471, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-6386178, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-7635193, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-7651408, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-7737504, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-7785336, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-8047169, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-8047170, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-8395004, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-8407824, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-8662543, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-8754838, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-9234737, http://linkedlifedata.com/resource/pubmed/commentcorrection/9851990-9244293
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Chromatin, http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSP40 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HsP104 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/SPT2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/SSA3 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Streptomyces trypsin inhibitor 1..., http://linkedlifedata.com/resource/pubmed/chemical/YDJ1 protein, S cerevisiae
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
180
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6484-92
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Suppression of an Hsp70 mutant phenotype in Saccharomyces cerevisiae through loss of function of the chromatin component Sin1p/Spt2p.
pubmed:affiliation
Department of Biomolecular Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
pubmed:publicationType
Journal Article
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