CENP-C and CENP-I are key connecting factors for kinetochore and CENP-A assembly
Although it is generally accepted that chromatin containing the histone H3 variant CENP-A is an epigenetic mark maintaining centromere identity, the pathways leading to the formation and maintenance of centromere chromatin remain unclear. We previously generated human artificial chromosomes (HACs) w...
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Veröffentlicht in: | Journal of cell science 2015-12, Vol.128 (24), p.4572-4587 |
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creator | Shono, Nobuaki Ohzeki, Jun-ichirou Otake, Koichiro Martins, Nuno M C Nagase, Takahiro Kimura, Hiroshi Larionov, Vladimir Earnshaw, William C Masumoto, Hiroshi |
description | Although it is generally accepted that chromatin containing the histone H3 variant CENP-A is an epigenetic mark maintaining centromere identity, the pathways leading to the formation and maintenance of centromere chromatin remain unclear. We previously generated human artificial chromosomes (HACs) whose centromeres contain a synthetic alpha-satellite (alphoid) DNA array containing the tetracycline operator (alphoid(tetO)). We also obtained cell lines bearing the alphoid(tetO) array at ectopic integration sites on chromosomal arms. Here, we have examined the regulation of CENP-A assembly at centromeres as well as de novo assembly on the ectopic arrays by tethering tetracycline repressor (tetR) fusions of substantial centromeric factors and chromatin modifiers. This analysis revealed four classes of factors that influence CENP-A assembly. Interestingly, many kinetochore structural components induced de novo CENP-A assembly at the ectopic site. We showed that these components work by recruiting CENP-C and subsequently recruiting M18BP1. Furthermore, we found that CENP-I can also recruit M18BP1 and, as a consequence, enhances M18BP1 assembly on centromeres in the downstream of CENP-C. Thus, we suggest that CENP-C and CENP-I are key factors connecting kinetochore to CENP-A assembly. |
doi_str_mv | 10.1242/jcs.180786 |
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We previously generated human artificial chromosomes (HACs) whose centromeres contain a synthetic alpha-satellite (alphoid) DNA array containing the tetracycline operator (alphoid(tetO)). We also obtained cell lines bearing the alphoid(tetO) array at ectopic integration sites on chromosomal arms. Here, we have examined the regulation of CENP-A assembly at centromeres as well as de novo assembly on the ectopic arrays by tethering tetracycline repressor (tetR) fusions of substantial centromeric factors and chromatin modifiers. This analysis revealed four classes of factors that influence CENP-A assembly. Interestingly, many kinetochore structural components induced de novo CENP-A assembly at the ectopic site. We showed that these components work by recruiting CENP-C and subsequently recruiting M18BP1. Furthermore, we found that CENP-I can also recruit M18BP1 and, as a consequence, enhances M18BP1 assembly on centromeres in the downstream of CENP-C. Thus, we suggest that CENP-C and CENP-I are key factors connecting kinetochore to CENP-A assembly.</description><identifier>ISSN: 0021-9533</identifier><identifier>ISSN: 1477-9137</identifier><identifier>EISSN: 1477-9137</identifier><identifier>DOI: 10.1242/jcs.180786</identifier><identifier>PMID: 26527398</identifier><language>eng</language><publisher>England: The Company of Biologists</publisher><subject>Autoantigens - genetics ; Autoantigens - metabolism ; Centromere Protein A ; Chromosomal Proteins, Non-Histone - genetics ; Chromosomal Proteins, Non-Histone - metabolism ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; HeLa Cells ; Humans ; Kinetochores - metabolism</subject><ispartof>Journal of cell science, 2015-12, Vol.128 (24), p.4572-4587</ispartof><rights>2015. Published by The Company of Biologists Ltd.</rights><rights>2015. 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We previously generated human artificial chromosomes (HACs) whose centromeres contain a synthetic alpha-satellite (alphoid) DNA array containing the tetracycline operator (alphoid(tetO)). We also obtained cell lines bearing the alphoid(tetO) array at ectopic integration sites on chromosomal arms. Here, we have examined the regulation of CENP-A assembly at centromeres as well as de novo assembly on the ectopic arrays by tethering tetracycline repressor (tetR) fusions of substantial centromeric factors and chromatin modifiers. This analysis revealed four classes of factors that influence CENP-A assembly. Interestingly, many kinetochore structural components induced de novo CENP-A assembly at the ectopic site. We showed that these components work by recruiting CENP-C and subsequently recruiting M18BP1. Furthermore, we found that CENP-I can also recruit M18BP1 and, as a consequence, enhances M18BP1 assembly on centromeres in the downstream of CENP-C. Thus, we suggest that CENP-C and CENP-I are key factors connecting kinetochore to CENP-A assembly.</description><subject>Autoantigens - genetics</subject><subject>Autoantigens - metabolism</subject><subject>Centromere Protein A</subject><subject>Chromosomal Proteins, Non-Histone - genetics</subject><subject>Chromosomal Proteins, Non-Histone - metabolism</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Kinetochores - metabolism</subject><issn>0021-9533</issn><issn>1477-9137</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkUFLAzEQhYMotlYv_gDJUYStmU02yV4EKVULoj3oOWSz03Z1u6nJVui_d7W16GkG5ps3j3mEnAMbQirS6zcXh6CZ0vKA9EEoleTA1SHpM5ZCkmec98hJjG-MMZXm6pj0Upmliue6T6aj8dM0GVHblPSnnVAbkL7jhjrfNOjaqpnTmXWtD5HOfKDvVYOtdwvfYfutW2pjxGVRb07J0czWEc92dUBe78Yvo4fk8fl-Mrp9TJzQuk00IFMoGctzl2LhSi5L4FIgFBlosCB4wQstgJWIUmOhILdCYiEyAZlwfEButrqrdbHE0mHTBlubVaiWNmyMt5X5P2mqhZn7TyNkLjPGOoHLnUDwH2uMrVlW0WFd2wb9OhpQHcWACejQqy3qgo8x4Gx_Bpj5jsB0EZhtBB188dfYHv39Of8CAqCAQA</recordid><startdate>20151215</startdate><enddate>20151215</enddate><creator>Shono, Nobuaki</creator><creator>Ohzeki, Jun-ichirou</creator><creator>Otake, Koichiro</creator><creator>Martins, Nuno M C</creator><creator>Nagase, Takahiro</creator><creator>Kimura, Hiroshi</creator><creator>Larionov, Vladimir</creator><creator>Earnshaw, William C</creator><creator>Masumoto, Hiroshi</creator><general>The Company of Biologists</general><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20151215</creationdate><title>CENP-C and CENP-I are key connecting factors for kinetochore and CENP-A assembly</title><author>Shono, Nobuaki ; Ohzeki, Jun-ichirou ; Otake, Koichiro ; Martins, Nuno M C ; Nagase, Takahiro ; Kimura, Hiroshi ; Larionov, Vladimir ; Earnshaw, William C ; Masumoto, Hiroshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c488t-81e07e60099c2ebcd36d1364e1b5181a143b3b8410dee68eb719a46eb454154c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Autoantigens - genetics</topic><topic>Autoantigens - metabolism</topic><topic>Centromere Protein A</topic><topic>Chromosomal Proteins, Non-Histone - genetics</topic><topic>Chromosomal Proteins, Non-Histone - metabolism</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Kinetochores - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shono, Nobuaki</creatorcontrib><creatorcontrib>Ohzeki, Jun-ichirou</creatorcontrib><creatorcontrib>Otake, Koichiro</creatorcontrib><creatorcontrib>Martins, Nuno M C</creatorcontrib><creatorcontrib>Nagase, Takahiro</creatorcontrib><creatorcontrib>Kimura, Hiroshi</creatorcontrib><creatorcontrib>Larionov, Vladimir</creatorcontrib><creatorcontrib>Earnshaw, William C</creatorcontrib><creatorcontrib>Masumoto, Hiroshi</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shono, Nobuaki</au><au>Ohzeki, Jun-ichirou</au><au>Otake, Koichiro</au><au>Martins, Nuno M C</au><au>Nagase, Takahiro</au><au>Kimura, Hiroshi</au><au>Larionov, Vladimir</au><au>Earnshaw, William C</au><au>Masumoto, Hiroshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>CENP-C and CENP-I are key connecting factors for kinetochore and CENP-A assembly</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>2015-12-15</date><risdate>2015</risdate><volume>128</volume><issue>24</issue><spage>4572</spage><epage>4587</epage><pages>4572-4587</pages><issn>0021-9533</issn><issn>1477-9137</issn><eissn>1477-9137</eissn><abstract>Although it is generally accepted that chromatin containing the histone H3 variant CENP-A is an epigenetic mark maintaining centromere identity, the pathways leading to the formation and maintenance of centromere chromatin remain unclear. We previously generated human artificial chromosomes (HACs) whose centromeres contain a synthetic alpha-satellite (alphoid) DNA array containing the tetracycline operator (alphoid(tetO)). We also obtained cell lines bearing the alphoid(tetO) array at ectopic integration sites on chromosomal arms. Here, we have examined the regulation of CENP-A assembly at centromeres as well as de novo assembly on the ectopic arrays by tethering tetracycline repressor (tetR) fusions of substantial centromeric factors and chromatin modifiers. This analysis revealed four classes of factors that influence CENP-A assembly. Interestingly, many kinetochore structural components induced de novo CENP-A assembly at the ectopic site. We showed that these components work by recruiting CENP-C and subsequently recruiting M18BP1. Furthermore, we found that CENP-I can also recruit M18BP1 and, as a consequence, enhances M18BP1 assembly on centromeres in the downstream of CENP-C. Thus, we suggest that CENP-C and CENP-I are key factors connecting kinetochore to CENP-A assembly.</abstract><cop>England</cop><pub>The Company of Biologists</pub><pmid>26527398</pmid><doi>10.1242/jcs.180786</doi><tpages>16</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Autoantigens - genetics Autoantigens - metabolism Centromere Protein A Chromosomal Proteins, Non-Histone - genetics Chromosomal Proteins, Non-Histone - metabolism DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism HeLa Cells Humans Kinetochores - metabolism |
title | CENP-C and CENP-I are key connecting factors for kinetochore and CENP-A assembly |
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