The Mub1/Ubr2 ubiquitin ligase complex regulates the conserved Dsn1 kinetochore protein
The kinetochore is the macromolecular complex that assembles onto centromeric DNA and orchestrates the segregation of duplicated chromosomes. More than 60 components make up the budding yeast kinetochore, including inner kinetochore proteins that bind to centromeric chromatin and outer proteins that...
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| creator | Akiyoshi, Bungo Nelson, Christian R Duggan, Nicole Ceto, Steven Ranish, Jeffrey A Biggins, Sue |
| description | The kinetochore is the macromolecular complex that assembles onto centromeric DNA and orchestrates the segregation of duplicated chromosomes. More than 60 components make up the budding yeast kinetochore, including inner kinetochore proteins that bind to centromeric chromatin and outer proteins that directly interact with microtubules. However, little is known about how these components assemble into a functional kinetochore and whether there are quality control mechanisms that monitor kinetochore integrity. We previously developed a method to isolate kinetochore particles via purification of the conserved Dsn1 kinetochore protein. We find that the Mub1/Ubr2 ubiquitin ligase complex associates with kinetochore particles through the CENP-C(Mif2) protein. Although Mub1/Ubr2 are not stable kinetochore components in vivo, they regulate the levels of the conserved outer kinetochore protein Dsn1 via ubiquitylation. Strikingly, a deletion of Mub1/Ubr2 restores the levels and viability of a mutant Dsn1 protein, reminiscent of quality control systems that target aberrant proteins for degradation. Consistent with this, Mub1/Ubr2 help to maintain viability when kinetochores are defective. Together, our data identify a previously unknown regulatory mechanism for the conserved Dsn1 kinetochore protein. We propose that Mub1/Ubr2 are part of a quality control system that monitors kinetochore integrity, thus ensuring genomic stability. |
| doi_str_mv | 10.1371/journal.pgen.1003216 |
| format | Article |
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More than 60 components make up the budding yeast kinetochore, including inner kinetochore proteins that bind to centromeric chromatin and outer proteins that directly interact with microtubules. However, little is known about how these components assemble into a functional kinetochore and whether there are quality control mechanisms that monitor kinetochore integrity. We previously developed a method to isolate kinetochore particles via purification of the conserved Dsn1 kinetochore protein. We find that the Mub1/Ubr2 ubiquitin ligase complex associates with kinetochore particles through the CENP-C(Mif2) protein. Although Mub1/Ubr2 are not stable kinetochore components in vivo, they regulate the levels of the conserved outer kinetochore protein Dsn1 via ubiquitylation. Strikingly, a deletion of Mub1/Ubr2 restores the levels and viability of a mutant Dsn1 protein, reminiscent of quality control systems that target aberrant proteins for degradation. Consistent with this, Mub1/Ubr2 help to maintain viability when kinetochores are defective. Together, our data identify a previously unknown regulatory mechanism for the conserved Dsn1 kinetochore protein. We propose that Mub1/Ubr2 are part of a quality control system that monitors kinetochore integrity, thus ensuring genomic stability.</description><identifier>ISSN: 1553-7404</identifier><identifier>ISSN: 1553-7390</identifier><identifier>EISSN: 1553-7404</identifier><identifier>DOI: 10.1371/journal.pgen.1003216</identifier><identifier>PMID: 23408894</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Biology ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell division ; Cell Survival - genetics ; Centromere - genetics ; Centromere - metabolism ; Chromatin - metabolism ; Chromosomal Proteins, Non-Histone - genetics ; Chromosomal Proteins, Non-Histone - metabolism ; Chromosomes ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Enzymes ; Experiments ; Gene expression ; Genetic aspects ; Health aspects ; Kinetochores ; Kinetochores - metabolism ; Ligases ; Physiological aspects ; Plasmids ; Proteins ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Ubiquitin ; Ubiquitin - genetics ; Ubiquitin - metabolism ; Ubiquitin-Protein Ligases - genetics ; Ubiquitin-Protein Ligases - metabolism ; Ubiquitination ; Yeast</subject><ispartof>PLoS genetics, 2013-02, Vol.9 (2), p.e1003216-e1003216</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Akiyoshi et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Akiyoshi B, Nelson CR, Duggan N, Ceto S, Ranish JA, et al. (2013) The Mub1/Ubr2 Ubiquitin Ligase Complex Regulates the Conserved Dsn1 Kinetochore Protein. PLoS Genet 9(2): e1003216. doi:10.1371/journal.pgen.1003216</rights><rights>2013 Akiyoshi et al 2013 Akiyoshi et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c726t-310da81bc2f184658c9bbda00c09fb0a5adb7450d8473fef0e83aa219caa55933</citedby><cites>FETCH-LOGICAL-c726t-310da81bc2f184658c9bbda00c09fb0a5adb7450d8473fef0e83aa219caa55933</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3567142/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3567142/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2100,2926,23865,27923,27924,53790,53792,79371,79372</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23408894$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Sullivan, Beth A.</contributor><creatorcontrib>Akiyoshi, Bungo</creatorcontrib><creatorcontrib>Nelson, Christian R</creatorcontrib><creatorcontrib>Duggan, Nicole</creatorcontrib><creatorcontrib>Ceto, Steven</creatorcontrib><creatorcontrib>Ranish, Jeffrey A</creatorcontrib><creatorcontrib>Biggins, Sue</creatorcontrib><title>The Mub1/Ubr2 ubiquitin ligase complex regulates the conserved Dsn1 kinetochore protein</title><title>PLoS genetics</title><addtitle>PLoS Genet</addtitle><description>The kinetochore is the macromolecular complex that assembles onto centromeric DNA and orchestrates the segregation of duplicated chromosomes. More than 60 components make up the budding yeast kinetochore, including inner kinetochore proteins that bind to centromeric chromatin and outer proteins that directly interact with microtubules. However, little is known about how these components assemble into a functional kinetochore and whether there are quality control mechanisms that monitor kinetochore integrity. We previously developed a method to isolate kinetochore particles via purification of the conserved Dsn1 kinetochore protein. We find that the Mub1/Ubr2 ubiquitin ligase complex associates with kinetochore particles through the CENP-C(Mif2) protein. Although Mub1/Ubr2 are not stable kinetochore components in vivo, they regulate the levels of the conserved outer kinetochore protein Dsn1 via ubiquitylation. Strikingly, a deletion of Mub1/Ubr2 restores the levels and viability of a mutant Dsn1 protein, reminiscent of quality control systems that target aberrant proteins for degradation. Consistent with this, Mub1/Ubr2 help to maintain viability when kinetochores are defective. Together, our data identify a previously unknown regulatory mechanism for the conserved Dsn1 kinetochore protein. We propose that Mub1/Ubr2 are part of a quality control system that monitors kinetochore integrity, thus ensuring genomic stability.</description><subject>Biology</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell division</subject><subject>Cell Survival - genetics</subject><subject>Centromere - genetics</subject><subject>Centromere - metabolism</subject><subject>Chromatin - metabolism</subject><subject>Chromosomal Proteins, Non-Histone - genetics</subject><subject>Chromosomal Proteins, Non-Histone - metabolism</subject><subject>Chromosomes</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Enzymes</subject><subject>Experiments</subject><subject>Gene expression</subject><subject>Genetic aspects</subject><subject>Health aspects</subject><subject>Kinetochores</subject><subject>Kinetochores - metabolism</subject><subject>Ligases</subject><subject>Physiological aspects</subject><subject>Plasmids</subject><subject>Proteins</subject><subject>Saccharomyces cerevisiae - 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More than 60 components make up the budding yeast kinetochore, including inner kinetochore proteins that bind to centromeric chromatin and outer proteins that directly interact with microtubules. However, little is known about how these components assemble into a functional kinetochore and whether there are quality control mechanisms that monitor kinetochore integrity. We previously developed a method to isolate kinetochore particles via purification of the conserved Dsn1 kinetochore protein. We find that the Mub1/Ubr2 ubiquitin ligase complex associates with kinetochore particles through the CENP-C(Mif2) protein. Although Mub1/Ubr2 are not stable kinetochore components in vivo, they regulate the levels of the conserved outer kinetochore protein Dsn1 via ubiquitylation. Strikingly, a deletion of Mub1/Ubr2 restores the levels and viability of a mutant Dsn1 protein, reminiscent of quality control systems that target aberrant proteins for degradation. Consistent with this, Mub1/Ubr2 help to maintain viability when kinetochores are defective. Together, our data identify a previously unknown regulatory mechanism for the conserved Dsn1 kinetochore protein. We propose that Mub1/Ubr2 are part of a quality control system that monitors kinetochore integrity, thus ensuring genomic stability.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23408894</pmid><doi>10.1371/journal.pgen.1003216</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Biology Carrier Proteins - genetics Carrier Proteins - metabolism Cell division Cell Survival - genetics Centromere - genetics Centromere - metabolism Chromatin - metabolism Chromosomal Proteins, Non-Histone - genetics Chromosomal Proteins, Non-Histone - metabolism Chromosomes DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Enzymes Experiments Gene expression Genetic aspects Health aspects Kinetochores Kinetochores - metabolism Ligases Physiological aspects Plasmids Proteins Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Ubiquitin Ubiquitin - genetics Ubiquitin - metabolism Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Ubiquitination Yeast |
| title | The Mub1/Ubr2 ubiquitin ligase complex regulates the conserved Dsn1 kinetochore protein |
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