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PMID: 9571234 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Saccharomyces cerevisiae cells with defective spindle pole body outer plaques accomplish nuclear migration via half-bridge-organized microtubules.

Molecular biology of the cell ·Vol. 9 ·No. 5 ·1998-05-00 ·Pages 977-91

Brachat A, Kilmartin JV, Wach A, Philippsen P

Abstract

Cnm67p, a novel yeast protein, localizes to the microtubule organizing center, the spindle pole body (SPB). Deletion of CNM67 (YNL225c) frequently results in spindle misorientation and impaired nuclear migration, leading to the generation of bi- and multinucleated cells (40%). Electron microscopy indicated that CNM67 is required for proper formation of the SPB outer plaque, a structure that nucleates cytoplasmic (astral) microtubules. Interestingly, cytoplasmic microtubules that are essential for spindle orientation and nuclear migration are still present in cnm67Delta1 cells that lack a detectable outer plaque. These microtubules are attached to the SPB half- bridge throughout the cell cycle. This interaction presumably allows for low-efficiency nuclear migration and thus provides a rescue mechanism in the absence of a functional outer plaque. Although CNM67 is not strictly required for mitosis, it is essential for sporulation. Time-lapse microscopy of cnm67Delta1 cells with green fluorescent protein (GFP)-labeled nuclei indicated that CNM67 is dispensable for nuclear migration (congression) and nuclear fusion during conjugation. This is in agreement with previous data, indicating that cytoplasmic microtubules are organized by the half-bridge during mating.

MeSH Terms
Benomyl/pharmacology Cell Nucleus/physiology Cytoskeleton Fungal Proteins/genetics,metabolism,physiology Fungicides, Industrial/pharmacology Microtubule-Associated Proteins/genetics,metabolism,physiology Microtubules/metabolism,physiology,ultrastructure Mutagenesis Saccharomyces cerevisiae/genetics,physiology,ultrastructure Spindle Apparatus/metabolism,physiology,ultrastructure Spores, Fungal
Chemicals
Fungal Proteins Fungicides, Industrial Microtubule-Associated Proteins Benomyl
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Brachat A
Lehrstuhl für Angewandte Mikrobiologie, Biozentrum, Universität Basel, CH-4056 Basel, Switzerland.
Kilmartin J V
Wach A
Philippsen P
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
Published
1998-05-00
Pages
977-91
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC25323
Subset
IM
Analysis Services
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