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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...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2002
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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. |
format | Text |
id | pubmed-2173979 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2002 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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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