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Recombination protein Tid1p controls resolution of cohesin-dependent linkages in meiosis in Saccharomyces cerevisiae
Sister chromatid cohesion and interhomologue recombination are coordinated to promote the segregation of homologous chromosomes instead of sister chromatids at the first meiotic division. During meiotic prophase in Saccharomyces cerevisiae, the meiosis-specific cohesin Rec8p localizes along chromoso...
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Published in: | The Journal of cell biology 2005-10, Vol.171 (2), p.241-253 |
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description | Sister chromatid cohesion and interhomologue recombination are coordinated to promote the segregation of homologous chromosomes instead of sister chromatids at the first meiotic division. During meiotic prophase in Saccharomyces cerevisiae, the meiosis-specific cohesin Rec8p localizes along chromosome axes and mediates most of the cohesion. The mitotic cohesin Mcd1p/Scc1p localizes to discrete spots along chromosome arms, and its function is not clear. In cells lacking Tid1p, which is a member of the SWI2/SNF2 family of helicase-like proteins that are involved in chromatin remodeling, Mcd1p and Rec8p persist abnormally through both meiotic divisions, and chromosome segregation fails in the majority of cells. Genetic results indicate that the primary defect in these cells is a failure to resolve Mcd1p-mediated connections. Tid1p interacts with recombination enzymes Dmc1p and Rad51p and has an established role in recombination repair. We propose that Tid1p remodels Mcd1p-mediated cohesion early in meiotic prophase to facilitate interhomologue recombination and the subsequent segregation of homologous chromosomes. |
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During meiotic prophase in Saccharomyces cerevisiae, the meiosis-specific cohesin Rec8p localizes along chromosome axes and mediates most of the cohesion. The mitotic cohesin Mcd1p/Scc1p localizes to discrete spots along chromosome arms, and its function is not clear. In cells lacking Tid1p, which is a member of the SWI2/SNF2 family of helicase-like proteins that are involved in chromatin remodeling, Mcd1p and Rec8p persist abnormally through both meiotic divisions, and chromosome segregation fails in the majority of cells. Genetic results indicate that the primary defect in these cells is a failure to resolve Mcd1p-mediated connections. Tid1p interacts with recombination enzymes Dmc1p and Rad51p and has an established role in recombination repair. We propose that Tid1p remodels Mcd1p-mediated cohesion early in meiotic prophase to facilitate interhomologue recombination and the subsequent segregation of homologous chromosomes.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200505020</identifier><identifier>PMID: 16230461</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Anaphase ; Anaphase - physiology ; Antibodies ; Cell Cycle Proteins - genetics ; Cell Cycle Proteins - metabolism ; Cell division ; Cell separation ; Cells ; Chromatids ; Chromatin ; Chromatin - metabolism ; Chromosomal Proteins, Non-Histone - genetics ; Chromosomal Proteins, Non-Histone - metabolism ; Chromosomes ; Chromosomes, Fungal - genetics ; Chromosomes, Fungal - metabolism ; Cohesins ; DNA Helicases ; DNA Repair Enzymes ; Dressers ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Genetics ; Meiosis ; Meiosis - physiology ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Pachytene stage ; Pachytene Stage - physiology ; Phosphoproteins - genetics ; Phosphoproteins - metabolism ; Proteins ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - physiology ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Sporulation</subject><ispartof>The Journal of cell biology, 2005-10, Vol.171 (2), p.241-253</ispartof><rights>Copyright 2005 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Oct 24, 2005</rights><rights>Copyright © 2005, The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c488t-dd1256b2f42adcefa8b7271f5588f125269e2ab23cc6c2987c2e9e826c23064f3</citedby><cites>FETCH-LOGICAL-c488t-dd1256b2f42adcefa8b7271f5588f125269e2ab23cc6c2987c2e9e826c23064f3</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/PMC2171180/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171180/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,733,786,790,891,27957,27958,53827,53829</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16230461$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kateneva, Anna V</creatorcontrib><creatorcontrib>Konovchenko, Anton A</creatorcontrib><creatorcontrib>Guacci, Vincent</creatorcontrib><creatorcontrib>Dresser, Michael E</creatorcontrib><title>Recombination protein Tid1p controls resolution of cohesin-dependent linkages in meiosis in Saccharomyces cerevisiae</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Sister chromatid cohesion and interhomologue recombination are coordinated to promote the segregation of homologous chromosomes instead of sister chromatids at the first meiotic division. During meiotic prophase in Saccharomyces cerevisiae, the meiosis-specific cohesin Rec8p localizes along chromosome axes and mediates most of the cohesion. The mitotic cohesin Mcd1p/Scc1p localizes to discrete spots along chromosome arms, and its function is not clear. In cells lacking Tid1p, which is a member of the SWI2/SNF2 family of helicase-like proteins that are involved in chromatin remodeling, Mcd1p and Rec8p persist abnormally through both meiotic divisions, and chromosome segregation fails in the majority of cells. Genetic results indicate that the primary defect in these cells is a failure to resolve Mcd1p-mediated connections. Tid1p interacts with recombination enzymes Dmc1p and Rad51p and has an established role in recombination repair. We propose that Tid1p remodels Mcd1p-mediated cohesion early in meiotic prophase to facilitate interhomologue recombination and the subsequent segregation of homologous chromosomes.</description><subject>Anaphase</subject><subject>Anaphase - physiology</subject><subject>Antibodies</subject><subject>Cell Cycle Proteins - genetics</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Cell division</subject><subject>Cell separation</subject><subject>Cells</subject><subject>Chromatids</subject><subject>Chromatin</subject><subject>Chromatin - metabolism</subject><subject>Chromosomal Proteins, Non-Histone - genetics</subject><subject>Chromosomal Proteins, Non-Histone - metabolism</subject><subject>Chromosomes</subject><subject>Chromosomes, Fungal - genetics</subject><subject>Chromosomes, Fungal - metabolism</subject><subject>Cohesins</subject><subject>DNA Helicases</subject><subject>DNA Repair Enzymes</subject><subject>Dressers</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Genetics</subject><subject>Meiosis</subject><subject>Meiosis - physiology</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>Pachytene stage</subject><subject>Pachytene Stage - physiology</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>Proteins</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - physiology</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Sporulation</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNqFkUtv1DAUhS0EokNhyQ5BxIJdyvV14ng2lVDFS6qERNu15Tg3Mx4SO9hJpf573M5oeGyQF36cz-f6-jD2ksMZByXe72x7hgB1HgiP2IrXFZSKV_CYrQCQl-sa6xP2LKUdAFRNJZ6yEy5RQCX5is3fyYaxdd7MLvhiimEm54tr1_GpsMHPMQypiJTCsDwQoc_HW0rOlx1N5DvyczE4_8NsKBX56kguJPewvDLWbk0M453NmqVIty45Q8_Zk94MiV4c5lN28-nj9cWX8vLb568XHy5LWyk1l13HsZYt9hWazlJvVNtgw_u6VqrPEso1oWlRWCstrlVjkdakMG8EyKoXp-x87zst7UjZIrdjBj1FN5p4p4Nx-m_Fu63ehFuNvOFcQTZ4dzCI4edCadajS5aGwXgKS9JSNcil4v8FERqBspIZfPsPuAtL9PkX7ovCWsi6zlC5h2wMKUXqj0_moO9T1zl1fUw986__7PM3fYg5A6_2wC7NIR71XExVgFl-s5d7E7TZRJf0zRUCF8BByEY24heBar0_</recordid><startdate>20051024</startdate><enddate>20051024</enddate><creator>Kateneva, Anna V</creator><creator>Konovchenko, Anton A</creator><creator>Guacci, Vincent</creator><creator>Dresser, Michael E</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20051024</creationdate><title>Recombination protein Tid1p controls resolution of cohesin-dependent linkages in meiosis in Saccharomyces cerevisiae</title><author>Kateneva, Anna V ; Konovchenko, Anton A ; Guacci, Vincent ; Dresser, Michael E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c488t-dd1256b2f42adcefa8b7271f5588f125269e2ab23cc6c2987c2e9e826c23064f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Anaphase</topic><topic>Anaphase - physiology</topic><topic>Antibodies</topic><topic>Cell Cycle Proteins - genetics</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Cell division</topic><topic>Cell separation</topic><topic>Cells</topic><topic>Chromatids</topic><topic>Chromatin</topic><topic>Chromatin - metabolism</topic><topic>Chromosomal Proteins, Non-Histone - genetics</topic><topic>Chromosomal Proteins, Non-Histone - metabolism</topic><topic>Chromosomes</topic><topic>Chromosomes, Fungal - genetics</topic><topic>Chromosomes, Fungal - metabolism</topic><topic>Cohesins</topic><topic>DNA Helicases</topic><topic>DNA Repair Enzymes</topic><topic>Dressers</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Genetics</topic><topic>Meiosis</topic><topic>Meiosis - physiology</topic><topic>Nuclear Proteins - genetics</topic><topic>Nuclear Proteins - metabolism</topic><topic>Pachytene stage</topic><topic>Pachytene Stage - physiology</topic><topic>Phosphoproteins - genetics</topic><topic>Phosphoproteins - metabolism</topic><topic>Proteins</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - physiology</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Sporulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kateneva, Anna V</creatorcontrib><creatorcontrib>Konovchenko, Anton A</creatorcontrib><creatorcontrib>Guacci, Vincent</creatorcontrib><creatorcontrib>Dresser, Michael E</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kateneva, Anna V</au><au>Konovchenko, Anton A</au><au>Guacci, Vincent</au><au>Dresser, Michael E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Recombination protein Tid1p controls resolution of cohesin-dependent linkages in meiosis in Saccharomyces cerevisiae</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2005-10-24</date><risdate>2005</risdate><volume>171</volume><issue>2</issue><spage>241</spage><epage>253</epage><pages>241-253</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><notes>Abbreviations used in this paper: DSB, double strand break; SC, synaptonemal complex; SPB, spindle pole body.</notes><notes>Correspondence to Michael E. Dresser: dresserm@omrf.ouhsc.edu</notes><abstract>Sister chromatid cohesion and interhomologue recombination are coordinated to promote the segregation of homologous chromosomes instead of sister chromatids at the first meiotic division. During meiotic prophase in Saccharomyces cerevisiae, the meiosis-specific cohesin Rec8p localizes along chromosome axes and mediates most of the cohesion. The mitotic cohesin Mcd1p/Scc1p localizes to discrete spots along chromosome arms, and its function is not clear. In cells lacking Tid1p, which is a member of the SWI2/SNF2 family of helicase-like proteins that are involved in chromatin remodeling, Mcd1p and Rec8p persist abnormally through both meiotic divisions, and chromosome segregation fails in the majority of cells. Genetic results indicate that the primary defect in these cells is a failure to resolve Mcd1p-mediated connections. Tid1p interacts with recombination enzymes Dmc1p and Rad51p and has an established role in recombination repair. We propose that Tid1p remodels Mcd1p-mediated cohesion early in meiotic prophase to facilitate interhomologue recombination and the subsequent segregation of homologous chromosomes.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>16230461</pmid><doi>10.1083/jcb.200505020</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Anaphase Anaphase - physiology Antibodies Cell Cycle Proteins - genetics Cell Cycle Proteins - metabolism Cell division Cell separation Cells Chromatids Chromatin Chromatin - metabolism Chromosomal Proteins, Non-Histone - genetics Chromosomal Proteins, Non-Histone - metabolism Chromosomes Chromosomes, Fungal - genetics Chromosomes, Fungal - metabolism Cohesins DNA Helicases DNA Repair Enzymes Dressers Fungal Proteins - genetics Fungal Proteins - metabolism Genetics Meiosis Meiosis - physiology Nuclear Proteins - genetics Nuclear Proteins - metabolism Pachytene stage Pachytene Stage - physiology Phosphoproteins - genetics Phosphoproteins - metabolism Proteins Recombinant Proteins - genetics Recombinant Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - physiology Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Sporulation |
title | Recombination protein Tid1p controls resolution of cohesin-dependent linkages in meiosis in Saccharomyces cerevisiae |
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