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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1997-2-3
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pubmed:databankReference | |
pubmed:abstractText |
A temperature-sensitive mutation (act1-1) in the essential actin gene of Saccharomyces cerevisiae can be suppressed by mutations in the SAC3 gene. A DNA fragment containing the SAC3 gene was sequenced. SAC3 codes for a 150 kDa hydrophillic protein which does not show any significant similarities with other proteins in the databases. Sac3 therefore is a novel yeast protein. A nuclear localization of Sac3 is suggested by the presence of a putative nuclear localization signal in the Sac3 sequence. A SAC3 disruption mutation was constructed. SAC3 disruption mutants were viable but grew more slowly and were larger than wild-type cells. In contrast to the sac3-1 mutation, the SAC3 disruption was not able to suppress the temperature sensitivity and the osmosensitivity of the act1-1 mutant. This demonstrates that act1-1 suppression by sac3-1 is not the result of a simple loss of SAC3 function. Furthermore, we examined the act1-1 and the sac3 mutants for defects in polarized cell growth by FITC-Concanavalin A (Con A)-labelling. The sac3 mutants showed a normal ConA-labelling pattern. In the act1-1 mutant, however, upon shift to non-permissive temperature, newly synthesized cell wall material, instead of being directed towards the bud, was deposited at discrete spots in the mother cell.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/AAC1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleocytoplasmic Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Porins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0749-503X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
965-75
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8873450-Actins,
pubmed-meshheading:8873450-Amino Acid Sequence,
pubmed-meshheading:8873450-Arabidopsis Proteins,
pubmed-meshheading:8873450-Base Sequence,
pubmed-meshheading:8873450-Genes, Fungal,
pubmed-meshheading:8873450-Genes, Suppressor,
pubmed-meshheading:8873450-Molecular Sequence Data,
pubmed-meshheading:8873450-Molecular Weight,
pubmed-meshheading:8873450-Mutation,
pubmed-meshheading:8873450-Nuclear Proteins,
pubmed-meshheading:8873450-Nucleocytoplasmic Transport Proteins,
pubmed-meshheading:8873450-Phenotype,
pubmed-meshheading:8873450-Porins,
pubmed-meshheading:8873450-Saccharomyces cerevisiae,
pubmed-meshheading:8873450-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8873450-Sequence Analysis, DNA,
pubmed-meshheading:8873450-Temperature
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pubmed:year |
1996
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pubmed:articleTitle |
Characterization of the SAC3 gene of Saccharomyces cerevisiae.
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pubmed:affiliation |
Institut für Mikrobiologie, Heinrich-Heine-Universität Düsseldorf, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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