Source:http://linkedlifedata.com/resource/pubmed/id/11405640
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2001-6-14
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pubmed:abstractText |
The SDS3 gene was identified in a suppressor screen for mutations that enhance position-effect silencing in yeast. Cells that are defective in SDS3 have pleiotropic phenotypes, similar to those seen in the absence of the histone deacetylase components Rpd3p and Sin3p, including meiotic defects and improper regulation of the HO gene. To gain further insight into SDS3 function we undertook an epistasis analysis with other SDS genes. We found that sds3 is synthetically lethal in combination with a deletion of the SWI6 (SDS11) gene, which encodes a cell-cycle regulator. sds3 swi6 double mutants do not display a specific cell-cycle arrest phenotype, but instead die due to cell lysis. Constitutive expression of the G1 cyclin gene CLN2 restores viability to an sds3 swi6 strain, as does overexpression of SKT5/ CHS4, which encodes a regulatory subunit of chitin synthase III, and SSD1, a gene previously implicated in ensuring cell-cycle progression and cellular integrity. Significantly, growth in the presence of 1 M sorbitol or overexpression of PKC1 also partially suppresses the lethal phenotype of the sds3 swi6 strain. This lethality in the absence of SWI6 function most probably reflects an important or essential role for Sds3p in the Rpd3p/Sin3p histone deacetylase complex, since RPD3 and SIN3 mutations are also synthetically lethal in combination with swi6 and these phenotypes are also rescued by elevated dosage of SKT5/CHS4, SSD1, or PCK1. Taken together, these data indicate that the transcription factor Swi6p and the Rpd3p-based deacetylase complex act in parallel pathways to activate genes required for cell wall biosynthesis.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carboxylic Ester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases,
http://linkedlifedata.com/resource/pubmed/chemical/RPD3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SIN3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SWI6 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1617-4615
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
265
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
560-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11405640-Carboxylic Ester Hydrolases,
pubmed-meshheading:11405640-Cell Division,
pubmed-meshheading:11405640-Cell Wall,
pubmed-meshheading:11405640-Fungal Proteins,
pubmed-meshheading:11405640-Gene Deletion,
pubmed-meshheading:11405640-Genetic Complementation Test,
pubmed-meshheading:11405640-Histone Deacetylases,
pubmed-meshheading:11405640-Meiosis,
pubmed-meshheading:11405640-Mutation,
pubmed-meshheading:11405640-Phenotype,
pubmed-meshheading:11405640-Protein Binding,
pubmed-meshheading:11405640-Repressor Proteins,
pubmed-meshheading:11405640-Saccharomyces cerevisiae,
pubmed-meshheading:11405640-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11405640-Transcription Factors
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pubmed:year |
2001
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pubmed:articleTitle |
A role for Sds3p, a component of the Rpd3p/Sin3p deacetylase complex, in maintaining cellular integrity in Saccharomyces cerevisiae.
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pubmed:affiliation |
Department of Microbiology, College of Physicians and Surgeons of Columbia University, New York, NY 10032, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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