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Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p

Accurate duplication of the Saccharomyces cerevisiae spindle pole body (SPB) is required for formation of a bipolar mitotic spindle. We identified mutants in SPB assembly by screening a temperature-sensitive collection of yeast for defects in SPB incorporation of a fluorescently marked integral SPB...

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Detalles Bibliográficos
Autores principales: Jaspersen, Sue L., Giddings, Thomas H., Winey, Mark
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2002
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173979/
https://www.ncbi.nlm.nih.gov/pubmed/12486115
http://dx.doi.org/10.1083/jcb.200208169
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author Jaspersen, Sue L.
Giddings, Thomas H.
Winey, Mark
author_facet Jaspersen, Sue L.
Giddings, Thomas H.
Winey, Mark
author_sort Jaspersen, Sue L.
collection PubMed
description Accurate duplication of the Saccharomyces cerevisiae spindle pole body (SPB) is required for formation of a bipolar mitotic spindle. We identified mutants in SPB assembly by screening a temperature-sensitive collection of yeast for defects in SPB incorporation of a fluorescently marked integral SPB component, Spc42p. One SPB assembly mutant contained a mutation in a previously uncharacterized open reading frame that we call MPS3 (for monopolar spindle). mps3-1 mutants arrest in mitosis with monopolar spindles at the nonpermissive temperature, suggesting a defect in SPB duplication. Execution point experiments revealed that MPS3 function is required for the first step of SPB duplication in G1. Like cells containing mutations in two other genes required for this step of SPB duplication (CDC31 and KAR1), mps3-1 mutants arrest with a single unduplicated SPB that lacks an associated half-bridge. MPS3 encodes an essential integral membrane protein that localizes to the SPB half-bridge. Genetic interactions between MPS3 and CDC31 and binding of Cdc31p to Mps3p in vitro, as well as the fact that Cdc31p localization to the SPB is partially dependent on Mps3p function, suggest that one function for Mps3p during SPB duplication is to recruit Cdc31p, the yeast centrin homologue, to the half-bridge.
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spelling pubmed-21739792008-05-01 Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p Jaspersen, Sue L. Giddings, Thomas H. Winey, Mark J Cell Biol Article Accurate duplication of the Saccharomyces cerevisiae spindle pole body (SPB) is required for formation of a bipolar mitotic spindle. We identified mutants in SPB assembly by screening a temperature-sensitive collection of yeast for defects in SPB incorporation of a fluorescently marked integral SPB component, Spc42p. One SPB assembly mutant contained a mutation in a previously uncharacterized open reading frame that we call MPS3 (for monopolar spindle). mps3-1 mutants arrest in mitosis with monopolar spindles at the nonpermissive temperature, suggesting a defect in SPB duplication. Execution point experiments revealed that MPS3 function is required for the first step of SPB duplication in G1. Like cells containing mutations in two other genes required for this step of SPB duplication (CDC31 and KAR1), mps3-1 mutants arrest with a single unduplicated SPB that lacks an associated half-bridge. MPS3 encodes an essential integral membrane protein that localizes to the SPB half-bridge. Genetic interactions between MPS3 and CDC31 and binding of Cdc31p to Mps3p in vitro, as well as the fact that Cdc31p localization to the SPB is partially dependent on Mps3p function, suggest that one function for Mps3p during SPB duplication is to recruit Cdc31p, the yeast centrin homologue, to the half-bridge. The Rockefeller University Press 2002-12-23 /pmc/articles/PMC2173979/ /pubmed/12486115 http://dx.doi.org/10.1083/jcb.200208169 Text en Copyright © 2002, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Jaspersen, Sue L.
Giddings, Thomas H.
Winey, Mark
Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p
title Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p
title_full Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p
title_fullStr Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p
title_full_unstemmed Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p
title_short Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p
title_sort mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue cdc31p
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173979/
https://www.ncbi.nlm.nih.gov/pubmed/12486115
http://dx.doi.org/10.1083/jcb.200208169
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