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Publication Detail
A role of Sep1 (= Kem1, Xrn1) as a microtubule-associated protein in Saccharomyces cerevisiae.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Interthal H, Bellocq C, Bähler J, Bashkirov VI, Edelstein S, Heyer WD
  • Publication date:
    15/03/1995
  • Pagination:
    1057, 1066
  • Journal:
    EMBO J
  • Volume:
    14
  • Issue:
    6
  • Status:
    Published
  • Country:
    England
  • Print ISSN:
    0261-4189
  • Language:
    eng
  • Keywords:
    Animals, Benomyl, Brain Chemistry, Cell Division, Cell Nucleus, DNA Mutational Analysis, Deoxyribonucleases, Epistasis, Genetic, Exoribonucleases, Fungal Proteins, Genes, Fungal, Microtubule-Associated Proteins, Microtubules, Nocodazole, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Spindle Apparatus, Swine, Tubulin
Abstract
Saccharomyces cerevisiae cells lacking the SEP1 (also known as XRN1, KEM1, DST2, RAR5) gene function exhibit a number of phenotypes in cellular processes related to microtubule function. Mutant cells show increased sensitivity to the microtubule-destabilizing drug benomyl, increased chromosome loss, a karyogamy defect, impaired spindle pole body separation, and defective nuclear migration towards the bud neck. Analysis of the arrest morphology and of the survival during arrest strongly suggests a structural defect accounting for the benomyl hypersensitivity, rather than a regulatory defect in a checkpoint. Biochemical analysis of the purified Sep1 protein demonstrates its ability to promote the polymerization of procine brain and authentic S.cerevisiae tubulin into flexible microtubules in vitro. Furthermore, Sep1 co-sediments with these microtubules in sucrose cushion centrifugation. Genetic analysis of double mutant strains containing a mutation in SEP1 and in one of the genes coding for alpha- or beta-tubulin further suggests interaction between Sep1 and microtubules. Taken together these three lines of evidence constitute compelling evidence for a role of Sep1 as an accessory protein in microtubule function in the yeast S.cerevisiae.
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