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Microtubule stability in budding yeast: characterization and dosage suppression of a benomyl-dependent tubulin mutant.
Machin, N A; Lee, J M; Barnes, G.
Afiliação
  • Machin NA; Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.
Mol Biol Cell ; 6(9): 1241-59, 1995 Sep.
Article em En | MEDLINE | ID: mdl-8534919
To better understand the dynamic regulation of microtubule structures in yeast, we studied a conditional-lethal beta-tubulin mutation tub2-150. This mutation is unique among the hundreds of tubulin mutations isolated in Saccharomyces cerevisiae in that it appears to cause an increase in the stability of microtubules. We report here that this allele is a mutation of threonine 238 to alanine, and that tub2-150 prevents the spindle from elongating during anaphase, suggesting a nuclear microtubule defect. To identify regulators of microtubule stability and/or anaphase, yeast genes were selected that, when overexpressed, could suppress the tub2-150 temperature-sensitive phenotype. One of these genes, JSN1, encodes a protein of 125 kDa that has limited similarity to a number of proteins of unknown function. Overexpression of the JSN1 gene in a TUB2 strain causes that strain to become more sensitive to benomyl, a microtubule-destabilizing drug. Of a representative group of microtubule mutants, only one other mutation, tub2-404, could be suppressed by JSN1 overexpression, showing that JSN1 is an allele-specific suppressor. As tub2-404 mutants are also defective for spindle elongation, this provides additional support for a role for JSN1 during anaphase.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Tubulina (Proteína) / Benomilo / Proteínas Fúngicas / Proteínas de Saccharomyces cerevisiae / Microtúbulos / Fuso Acromático Limite: Animals Idioma: En Revista: Mol Biol Cell Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 1995 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Tubulina (Proteína) / Benomilo / Proteínas Fúngicas / Proteínas de Saccharomyces cerevisiae / Microtúbulos / Fuso Acromático Limite: Animals Idioma: En Revista: Mol Biol Cell Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 1995 Tipo de documento: Article País de afiliação: Estados Unidos