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 porcine 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 α- or β-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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1057-1066 |
| Number of pages | 10 |
| Journal | EMBO Journal |
| Volume | 14 |
| Issue number | 6 |
| State | Published - 1995 |
| Externally published | Yes |
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Keywords
- Benomyl
- MAP
- Spindle pole body
- Tubulin
- Yeast
ASJC Scopus subject areas
- Cell Biology
- Genetics
Cite this
A role of Sep1 (= Kem1, Xrn1) as a microtubule-associated protein in Saccharomyces cerevisiae. / Interthal, H.; Bellocq, C.; Bahler, J.; Bashkirov, V. I.; Edelstein, S.; Heyer, W. D.
In: EMBO Journal, Vol. 14, No. 6, 1995, p. 1057-1066.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A role of Sep1 (= Kem1, Xrn1) as a microtubule-associated protein in Saccharomyces cerevisiae
AU - Interthal, H.
AU - Bellocq, C.
AU - Bahler, J.
AU - Bashkirov, V. I.
AU - Edelstein, S.
AU - Heyer, W. D.
PY - 1995
Y1 - 1995
N2 - 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 porcine 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 α- or β-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.
AB - 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 porcine 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 α- or β-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.
KW - Benomyl
KW - MAP
KW - Spindle pole body
KW - Tubulin
KW - Yeast
UR - http://www.scopus.com/inward/record.url?scp=0028912794&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028912794&partnerID=8YFLogxK
M3 - Article
VL - 14
SP - 1057
EP - 1066
JO - EMBO Journal
JF - EMBO Journal
SN - 0261-4189
IS - 6
ER -