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Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization
The Saccharomyces cerevisiae SUN-domain protein Mps3 is required for duplication of the yeast centrosome-equivalent organelle, the spindle pole body (SPB), and it is involved in multiple aspects of nuclear organization, including telomere tethering and gene silencing at the nuclear membrane, establi...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The American Society for Cell Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3386218/ https://www.ncbi.nlm.nih.gov/pubmed/22593213 http://dx.doi.org/10.1091/mbc.E11-07-0600 |
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author | Ghosh, Suman Gardner, Jennifer M. Smoyer, Christine J. Friederichs, Jennifer M. Unruh, Jay R. Slaughter, Brian D. Alexander, Richard Chisholm, Robert D. Lee, Kenneth K. Workman, Jerry L. Jaspersen, Sue L. |
author_facet | Ghosh, Suman Gardner, Jennifer M. Smoyer, Christine J. Friederichs, Jennifer M. Unruh, Jay R. Slaughter, Brian D. Alexander, Richard Chisholm, Robert D. Lee, Kenneth K. Workman, Jerry L. Jaspersen, Sue L. |
author_sort | Ghosh, Suman |
collection | PubMed |
description | The Saccharomyces cerevisiae SUN-domain protein Mps3 is required for duplication of the yeast centrosome-equivalent organelle, the spindle pole body (SPB), and it is involved in multiple aspects of nuclear organization, including telomere tethering and gene silencing at the nuclear membrane, establishment of sister chromatid cohesion, and repair of certain types of persistent DNA double-stranded breaks. How these diverse SUN protein functions are regulated is unknown. Here we show that the Mps3 N-terminus is a substrate for the acetyltransferase Eco1/Ctf7 in vitro and in vivo and map the sites of acetylation to three lysine residues adjacent to the Mps3 transmembrane domain. Mutation of these residues shows that acetylation is not essential for growth, SPB duplication, or distribution in the nuclear membrane. However, analysis of nonacetylatable mps3 mutants shows that this modification is required for accurate sister chromatid cohesion and for chromosome recruitment to the nuclear membrane. Acetylation of Mps3 by Eco1 is one of the few regulatory mechanisms known to control nuclear organization. |
format | Online Article Text |
id | pubmed-3386218 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-33862182012-09-16 Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization Ghosh, Suman Gardner, Jennifer M. Smoyer, Christine J. Friederichs, Jennifer M. Unruh, Jay R. Slaughter, Brian D. Alexander, Richard Chisholm, Robert D. Lee, Kenneth K. Workman, Jerry L. Jaspersen, Sue L. Mol Biol Cell Articles The Saccharomyces cerevisiae SUN-domain protein Mps3 is required for duplication of the yeast centrosome-equivalent organelle, the spindle pole body (SPB), and it is involved in multiple aspects of nuclear organization, including telomere tethering and gene silencing at the nuclear membrane, establishment of sister chromatid cohesion, and repair of certain types of persistent DNA double-stranded breaks. How these diverse SUN protein functions are regulated is unknown. Here we show that the Mps3 N-terminus is a substrate for the acetyltransferase Eco1/Ctf7 in vitro and in vivo and map the sites of acetylation to three lysine residues adjacent to the Mps3 transmembrane domain. Mutation of these residues shows that acetylation is not essential for growth, SPB duplication, or distribution in the nuclear membrane. However, analysis of nonacetylatable mps3 mutants shows that this modification is required for accurate sister chromatid cohesion and for chromosome recruitment to the nuclear membrane. Acetylation of Mps3 by Eco1 is one of the few regulatory mechanisms known to control nuclear organization. The American Society for Cell Biology 2012-07-01 /pmc/articles/PMC3386218/ /pubmed/22593213 http://dx.doi.org/10.1091/mbc.E11-07-0600 Text en © 2012 Ghosh et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell BD; are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Ghosh, Suman Gardner, Jennifer M. Smoyer, Christine J. Friederichs, Jennifer M. Unruh, Jay R. Slaughter, Brian D. Alexander, Richard Chisholm, Robert D. Lee, Kenneth K. Workman, Jerry L. Jaspersen, Sue L. Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization |
title | Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization |
title_full | Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization |
title_fullStr | Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization |
title_full_unstemmed | Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization |
title_short | Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization |
title_sort | acetylation of the sun protein mps3 by eco1 regulates its function in nuclear organization |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3386218/ https://www.ncbi.nlm.nih.gov/pubmed/22593213 http://dx.doi.org/10.1091/mbc.E11-07-0600 |
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