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A novel mechanism for the establishment of sister chromatid cohesion by the ECO1 acetyltransferase
Cohesin complex mediates cohesion between sister chromatids, which promotes high-fidelity chromosome segregation. Eco1p acetylates the cohesin subunit Smc3p during S phase to establish cohesion. The current model posits that this Eco1p-mediated acetylation promotes establishment by abrogating the ab...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4279223/ https://www.ncbi.nlm.nih.gov/pubmed/25378582 http://dx.doi.org/10.1091/mbc.E14-08-1268 |
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author | Guacci, Vincent Stricklin, Jeremiah Bloom, Michelle S. Guō, Xuánzōng Bhatter, Meghna Koshland, Douglas |
author_facet | Guacci, Vincent Stricklin, Jeremiah Bloom, Michelle S. Guō, Xuánzōng Bhatter, Meghna Koshland, Douglas |
author_sort | Guacci, Vincent |
collection | PubMed |
description | Cohesin complex mediates cohesion between sister chromatids, which promotes high-fidelity chromosome segregation. Eco1p acetylates the cohesin subunit Smc3p during S phase to establish cohesion. The current model posits that this Eco1p-mediated acetylation promotes establishment by abrogating the ability of Wpl1p to destabilize cohesin binding to chromosomes. Here we present data from budding yeast that is incompatible with this Wpl1p-centric model. Two independent in vivo assays show that a wpl1∆ fails to suppress cohesion defects of eco1∆ cells. Moreover, a wpl1∆ also fails to suppress cohesion defects engendered by blocking just the essential Eco1p acetylation sites on Smc3p (K112, K113). Thus removing WPL1 inhibition is insufficient for generating cohesion without ECO1 activity. To elucidate how ECO1 promotes cohesion, we conducted a genetic screen and identified a cohesion activator mutation in the SMC3 head domain (D1189H). Smc3-D1189H partially restores cohesion in eco1∆ wpl1∆ or eco1 mutant cells but robustly restores cohesion in cells blocked for Smc3p K112 K113 acetylation. These data support two important conclusions. First, acetylation of the K112 K113 region by Eco1p promotes cohesion establishment by altering Smc3p head function independent of its ability to antagonize Wpl1p. Second, Eco1p targets other than Smc3p K112 K113 are necessary for efficient establishment. |
format | Online Article Text |
id | pubmed-4279223 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-42792232015-03-16 A novel mechanism for the establishment of sister chromatid cohesion by the ECO1 acetyltransferase Guacci, Vincent Stricklin, Jeremiah Bloom, Michelle S. Guō, Xuánzōng Bhatter, Meghna Koshland, Douglas Mol Biol Cell Articles Cohesin complex mediates cohesion between sister chromatids, which promotes high-fidelity chromosome segregation. Eco1p acetylates the cohesin subunit Smc3p during S phase to establish cohesion. The current model posits that this Eco1p-mediated acetylation promotes establishment by abrogating the ability of Wpl1p to destabilize cohesin binding to chromosomes. Here we present data from budding yeast that is incompatible with this Wpl1p-centric model. Two independent in vivo assays show that a wpl1∆ fails to suppress cohesion defects of eco1∆ cells. Moreover, a wpl1∆ also fails to suppress cohesion defects engendered by blocking just the essential Eco1p acetylation sites on Smc3p (K112, K113). Thus removing WPL1 inhibition is insufficient for generating cohesion without ECO1 activity. To elucidate how ECO1 promotes cohesion, we conducted a genetic screen and identified a cohesion activator mutation in the SMC3 head domain (D1189H). Smc3-D1189H partially restores cohesion in eco1∆ wpl1∆ or eco1 mutant cells but robustly restores cohesion in cells blocked for Smc3p K112 K113 acetylation. These data support two important conclusions. First, acetylation of the K112 K113 region by Eco1p promotes cohesion establishment by altering Smc3p head function independent of its ability to antagonize Wpl1p. Second, Eco1p targets other than Smc3p K112 K113 are necessary for efficient establishment. The American Society for Cell Biology 2015-01-01 /pmc/articles/PMC4279223/ /pubmed/25378582 http://dx.doi.org/10.1091/mbc.E14-08-1268 Text en © 2015 Guacci 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 for Cell Biology. |
spellingShingle | Articles Guacci, Vincent Stricklin, Jeremiah Bloom, Michelle S. Guō, Xuánzōng Bhatter, Meghna Koshland, Douglas A novel mechanism for the establishment of sister chromatid cohesion by the ECO1 acetyltransferase |
title | A novel mechanism for the establishment of sister chromatid cohesion by the ECO1 acetyltransferase |
title_full | A novel mechanism for the establishment of sister chromatid cohesion by the ECO1 acetyltransferase |
title_fullStr | A novel mechanism for the establishment of sister chromatid cohesion by the ECO1 acetyltransferase |
title_full_unstemmed | A novel mechanism for the establishment of sister chromatid cohesion by the ECO1 acetyltransferase |
title_short | A novel mechanism for the establishment of sister chromatid cohesion by the ECO1 acetyltransferase |
title_sort | novel mechanism for the establishment of sister chromatid cohesion by the eco1 acetyltransferase |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4279223/ https://www.ncbi.nlm.nih.gov/pubmed/25378582 http://dx.doi.org/10.1091/mbc.E14-08-1268 |
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