Sfh1, an essential component of the RSC chromatin remodeling complex, maintains genome integrity in fission yeast

Abp1 is a fission yeast CENP‐B homologue that contributes to centromere function, silencing at pericentromeric heterochromatin and silencing of retrotransposons. We identified the sfh1 gene, encoding a core subunit of the fission yeast chromatin remodeling complex RSC as an Abp1‐interacting protein....

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Genes to cells : devoted to molecular & cellular mechanisms 2018-09, Vol.23 (9), p.738-752
Hauptverfasser: Kotomura, Naoe, Tsunemine, Satoru, Kuragano, Masahiro, Asanuma, Takahiro, Nakagawa, Hiromi, Tanaka, Katsunori, Murakami, Yota
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 752
container_issue 9
container_start_page 738
container_title Genes to cells : devoted to molecular & cellular mechanisms
container_volume 23
creator Kotomura, Naoe
Tsunemine, Satoru
Kuragano, Masahiro
Asanuma, Takahiro
Nakagawa, Hiromi
Tanaka, Katsunori
Murakami, Yota
description Abp1 is a fission yeast CENP‐B homologue that contributes to centromere function, silencing at pericentromeric heterochromatin and silencing of retrotransposons. We identified the sfh1 gene, encoding a core subunit of the fission yeast chromatin remodeling complex RSC as an Abp1‐interacting protein. Because sfh1 is essential for growth, we isolated temperature‐sensitive sfh1 mutants. These mutants showed defects in centromere functions, reflected by sensitivity to an inhibitor of spindle formation and minichromosome instability. Sfh1 localized at both kinetochore and pericentromeric heterochromatin regions. Although sfh1 mutations had minor effect on silencing at these regions, they decreased the levels of cohesin on centromeric heterochromatin. Sfh1 also localized at a retrotransposon, Tf2, in a partly Abp1‐dependent manner, and assisted in silencing of Tf2 by Abp1 probably in the same pathway as a histone chaperon, HIRA, which is also known to involve in Tf2 repression. Furthermore, sfh1 mutants were sensitive to several DNA‐damaging treatments (HU, MMS, UV and X‐ray). Increase in spontaneous foci of Rad22, a recombination Mediator protein Rad52 homologue, in sfh1 mutant suggests that RSC functions in homologous recombination repair of double‐stranded break downstream of the Rad22 recruitment. These results indicate that RSC plays multiple roles in the maintenance of genome integrity. We isolated Sfh1, an essential component of chromatin remodeler RSC, as a binding protein of CENP‐B homologue Abp1. Analysis of temperature‐sensitive mutant of Sfh1 showed that Sfh1/RSC involved in double‐strand DNA break repair, cohesin loading at pericetromere and repression of retrotransposons, which shows Sfh1/RSC plays an important role to maintain genome integrity.
doi_str_mv 10.1111/gtc.12629
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2096550922</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2100368308</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4549-9a62d7b95e0ff554c0ef6487fb0d2ec2e319f500d03629f6409a9f0b668c27623</originalsourceid><addsrcrecordid>eNp1kU1rGzEQhkVpSNwkh_6BIuglhWwy0q5k6xhMmxYMgXychawd2Qq7ki2tSfzvI9tpD4UMDDODHl5p9BLylcEVK3G9GOwV45KrT2TEaikq3jT1510vZKWEGp-QLzk_A7CagzgmJzUwIVTDR2T94JbskppAMWcMgzcdtbFfxVAGGh0dlkjvH6bULlPszeADTdjHFjsfFnuyw9dL2hsfhpKZLjDEHmkZcZH8sC0ddT5nHwPdosnDGTlypst4_l5PydOvn4_T39Xs7vbP9GZW2UY0qlJG8nY8VwLBOSEaC-hkMxm7ObQcLceaKScAWqjL4uUIlFEO5lJOLB9LXp-Si4PuKsX1BvOge58tdp0JGDdZc1BSCFB8h37_D32OmxTK6zRnUC6Y1DAp1I8DZVPMOaHTq-R7k7aagd75oIsPeu9DYb-9K27mPbb_yL8fX4DrA_DiO9x-rKRvH6cHyTf_zJFA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2100368308</pqid></control><display><type>article</type><title>Sfh1, an essential component of the RSC chromatin remodeling complex, maintains genome integrity in fission yeast</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Wiley Free Content</source><creator>Kotomura, Naoe ; Tsunemine, Satoru ; Kuragano, Masahiro ; Asanuma, Takahiro ; Nakagawa, Hiromi ; Tanaka, Katsunori ; Murakami, Yota</creator><creatorcontrib>Kotomura, Naoe ; Tsunemine, Satoru ; Kuragano, Masahiro ; Asanuma, Takahiro ; Nakagawa, Hiromi ; Tanaka, Katsunori ; Murakami, Yota</creatorcontrib><description>Abp1 is a fission yeast CENP‐B homologue that contributes to centromere function, silencing at pericentromeric heterochromatin and silencing of retrotransposons. We identified the sfh1 gene, encoding a core subunit of the fission yeast chromatin remodeling complex RSC as an Abp1‐interacting protein. Because sfh1 is essential for growth, we isolated temperature‐sensitive sfh1 mutants. These mutants showed defects in centromere functions, reflected by sensitivity to an inhibitor of spindle formation and minichromosome instability. Sfh1 localized at both kinetochore and pericentromeric heterochromatin regions. Although sfh1 mutations had minor effect on silencing at these regions, they decreased the levels of cohesin on centromeric heterochromatin. Sfh1 also localized at a retrotransposon, Tf2, in a partly Abp1‐dependent manner, and assisted in silencing of Tf2 by Abp1 probably in the same pathway as a histone chaperon, HIRA, which is also known to involve in Tf2 repression. Furthermore, sfh1 mutants were sensitive to several DNA‐damaging treatments (HU, MMS, UV and X‐ray). Increase in spontaneous foci of Rad22, a recombination Mediator protein Rad52 homologue, in sfh1 mutant suggests that RSC functions in homologous recombination repair of double‐stranded break downstream of the Rad22 recruitment. These results indicate that RSC plays multiple roles in the maintenance of genome integrity. We isolated Sfh1, an essential component of chromatin remodeler RSC, as a binding protein of CENP‐B homologue Abp1. Analysis of temperature‐sensitive mutant of Sfh1 showed that Sfh1/RSC involved in double‐strand DNA break repair, cohesin loading at pericetromere and repression of retrotransposons, which shows Sfh1/RSC plays an important role to maintain genome integrity.</description><identifier>ISSN: 1356-9597</identifier><identifier>EISSN: 1365-2443</identifier><identifier>DOI: 10.1111/gtc.12629</identifier><identifier>PMID: 30155942</identifier><language>eng</language><publisher>England: Wiley Subscription Services, Inc</publisher><subject>Cell Cycle Proteins - genetics ; Cell Cycle Proteins - metabolism ; Centromere ; Chromatin Assembly and Disassembly ; Chromatin remodeling ; Chromosomal Proteins, Non-Histone - genetics ; Chromosomal Proteins, Non-Histone - metabolism ; Chromosome Segregation ; Cohesin ; Cohesins ; DNA damage ; Gene Expression Regulation, Fungal ; Genomes ; Genomic Instability ; Heterochromatin ; Homologous recombination ; Homologous recombination repair ; Mediator protein ; Mutation ; Rad52 protein ; Retroelements ; Schizosaccharomyces - genetics ; Schizosaccharomyces pombe Proteins - genetics ; Schizosaccharomyces pombe Proteins - metabolism ; Ultraviolet radiation ; Yeast</subject><ispartof>Genes to cells : devoted to molecular &amp; cellular mechanisms, 2018-09, Vol.23 (9), p.738-752</ispartof><rights>2018 Molecular Biology Society of Japan and John Wiley &amp; Sons Australia, Ltd</rights><rights>2018 Molecular Biology Society of Japan and John Wiley &amp; Sons Australia, Ltd.</rights><rights>Copyright © 2018 Molecular Biology Society of Japan and John Wiley &amp; Sons Australia, Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4549-9a62d7b95e0ff554c0ef6487fb0d2ec2e319f500d03629f6409a9f0b668c27623</citedby><cites>FETCH-LOGICAL-c4549-9a62d7b95e0ff554c0ef6487fb0d2ec2e319f500d03629f6409a9f0b668c27623</cites><orcidid>0000-0002-2023-1303</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fgtc.12629$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fgtc.12629$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,778,782,1414,1430,27907,27908,45557,45558,46392,46816</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30155942$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kotomura, Naoe</creatorcontrib><creatorcontrib>Tsunemine, Satoru</creatorcontrib><creatorcontrib>Kuragano, Masahiro</creatorcontrib><creatorcontrib>Asanuma, Takahiro</creatorcontrib><creatorcontrib>Nakagawa, Hiromi</creatorcontrib><creatorcontrib>Tanaka, Katsunori</creatorcontrib><creatorcontrib>Murakami, Yota</creatorcontrib><title>Sfh1, an essential component of the RSC chromatin remodeling complex, maintains genome integrity in fission yeast</title><title>Genes to cells : devoted to molecular &amp; cellular mechanisms</title><addtitle>Genes Cells</addtitle><description>Abp1 is a fission yeast CENP‐B homologue that contributes to centromere function, silencing at pericentromeric heterochromatin and silencing of retrotransposons. We identified the sfh1 gene, encoding a core subunit of the fission yeast chromatin remodeling complex RSC as an Abp1‐interacting protein. Because sfh1 is essential for growth, we isolated temperature‐sensitive sfh1 mutants. These mutants showed defects in centromere functions, reflected by sensitivity to an inhibitor of spindle formation and minichromosome instability. Sfh1 localized at both kinetochore and pericentromeric heterochromatin regions. Although sfh1 mutations had minor effect on silencing at these regions, they decreased the levels of cohesin on centromeric heterochromatin. Sfh1 also localized at a retrotransposon, Tf2, in a partly Abp1‐dependent manner, and assisted in silencing of Tf2 by Abp1 probably in the same pathway as a histone chaperon, HIRA, which is also known to involve in Tf2 repression. Furthermore, sfh1 mutants were sensitive to several DNA‐damaging treatments (HU, MMS, UV and X‐ray). Increase in spontaneous foci of Rad22, a recombination Mediator protein Rad52 homologue, in sfh1 mutant suggests that RSC functions in homologous recombination repair of double‐stranded break downstream of the Rad22 recruitment. These results indicate that RSC plays multiple roles in the maintenance of genome integrity. We isolated Sfh1, an essential component of chromatin remodeler RSC, as a binding protein of CENP‐B homologue Abp1. Analysis of temperature‐sensitive mutant of Sfh1 showed that Sfh1/RSC involved in double‐strand DNA break repair, cohesin loading at pericetromere and repression of retrotransposons, which shows Sfh1/RSC plays an important role to maintain genome integrity.</description><subject>Cell Cycle Proteins - genetics</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Centromere</subject><subject>Chromatin Assembly and Disassembly</subject><subject>Chromatin remodeling</subject><subject>Chromosomal Proteins, Non-Histone - genetics</subject><subject>Chromosomal Proteins, Non-Histone - metabolism</subject><subject>Chromosome Segregation</subject><subject>Cohesin</subject><subject>Cohesins</subject><subject>DNA damage</subject><subject>Gene Expression Regulation, Fungal</subject><subject>Genomes</subject><subject>Genomic Instability</subject><subject>Heterochromatin</subject><subject>Homologous recombination</subject><subject>Homologous recombination repair</subject><subject>Mediator protein</subject><subject>Mutation</subject><subject>Rad52 protein</subject><subject>Retroelements</subject><subject>Schizosaccharomyces - genetics</subject><subject>Schizosaccharomyces pombe Proteins - genetics</subject><subject>Schizosaccharomyces pombe Proteins - metabolism</subject><subject>Ultraviolet radiation</subject><subject>Yeast</subject><issn>1356-9597</issn><issn>1365-2443</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kU1rGzEQhkVpSNwkh_6BIuglhWwy0q5k6xhMmxYMgXychawd2Qq7ki2tSfzvI9tpD4UMDDODHl5p9BLylcEVK3G9GOwV45KrT2TEaikq3jT1510vZKWEGp-QLzk_A7CagzgmJzUwIVTDR2T94JbskppAMWcMgzcdtbFfxVAGGh0dlkjvH6bULlPszeADTdjHFjsfFnuyw9dL2hsfhpKZLjDEHmkZcZH8sC0ddT5nHwPdosnDGTlypst4_l5PydOvn4_T39Xs7vbP9GZW2UY0qlJG8nY8VwLBOSEaC-hkMxm7ObQcLceaKScAWqjL4uUIlFEO5lJOLB9LXp-Si4PuKsX1BvOge58tdp0JGDdZc1BSCFB8h37_D32OmxTK6zRnUC6Y1DAp1I8DZVPMOaHTq-R7k7aagd75oIsPeu9DYb-9K27mPbb_yL8fX4DrA_DiO9x-rKRvH6cHyTf_zJFA</recordid><startdate>201809</startdate><enddate>201809</enddate><creator>Kotomura, Naoe</creator><creator>Tsunemine, Satoru</creator><creator>Kuragano, Masahiro</creator><creator>Asanuma, Takahiro</creator><creator>Nakagawa, Hiromi</creator><creator>Tanaka, Katsunori</creator><creator>Murakami, Yota</creator><general>Wiley Subscription Services, Inc</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>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-2023-1303</orcidid></search><sort><creationdate>201809</creationdate><title>Sfh1, an essential component of the RSC chromatin remodeling complex, maintains genome integrity in fission yeast</title><author>Kotomura, Naoe ; Tsunemine, Satoru ; Kuragano, Masahiro ; Asanuma, Takahiro ; Nakagawa, Hiromi ; Tanaka, Katsunori ; Murakami, Yota</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4549-9a62d7b95e0ff554c0ef6487fb0d2ec2e319f500d03629f6409a9f0b668c27623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Cell Cycle Proteins - genetics</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Centromere</topic><topic>Chromatin Assembly and Disassembly</topic><topic>Chromatin remodeling</topic><topic>Chromosomal Proteins, Non-Histone - genetics</topic><topic>Chromosomal Proteins, Non-Histone - metabolism</topic><topic>Chromosome Segregation</topic><topic>Cohesin</topic><topic>Cohesins</topic><topic>DNA damage</topic><topic>Gene Expression Regulation, Fungal</topic><topic>Genomes</topic><topic>Genomic Instability</topic><topic>Heterochromatin</topic><topic>Homologous recombination</topic><topic>Homologous recombination repair</topic><topic>Mediator protein</topic><topic>Mutation</topic><topic>Rad52 protein</topic><topic>Retroelements</topic><topic>Schizosaccharomyces - genetics</topic><topic>Schizosaccharomyces pombe Proteins - genetics</topic><topic>Schizosaccharomyces pombe Proteins - metabolism</topic><topic>Ultraviolet radiation</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kotomura, Naoe</creatorcontrib><creatorcontrib>Tsunemine, Satoru</creatorcontrib><creatorcontrib>Kuragano, Masahiro</creatorcontrib><creatorcontrib>Asanuma, Takahiro</creatorcontrib><creatorcontrib>Nakagawa, Hiromi</creatorcontrib><creatorcontrib>Tanaka, Katsunori</creatorcontrib><creatorcontrib>Murakami, Yota</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Genes to cells : devoted to molecular &amp; cellular mechanisms</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kotomura, Naoe</au><au>Tsunemine, Satoru</au><au>Kuragano, Masahiro</au><au>Asanuma, Takahiro</au><au>Nakagawa, Hiromi</au><au>Tanaka, Katsunori</au><au>Murakami, Yota</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sfh1, an essential component of the RSC chromatin remodeling complex, maintains genome integrity in fission yeast</atitle><jtitle>Genes to cells : devoted to molecular &amp; cellular mechanisms</jtitle><addtitle>Genes Cells</addtitle><date>2018-09</date><risdate>2018</risdate><volume>23</volume><issue>9</issue><spage>738</spage><epage>752</epage><pages>738-752</pages><issn>1356-9597</issn><eissn>1365-2443</eissn><abstract>Abp1 is a fission yeast CENP‐B homologue that contributes to centromere function, silencing at pericentromeric heterochromatin and silencing of retrotransposons. We identified the sfh1 gene, encoding a core subunit of the fission yeast chromatin remodeling complex RSC as an Abp1‐interacting protein. Because sfh1 is essential for growth, we isolated temperature‐sensitive sfh1 mutants. These mutants showed defects in centromere functions, reflected by sensitivity to an inhibitor of spindle formation and minichromosome instability. Sfh1 localized at both kinetochore and pericentromeric heterochromatin regions. Although sfh1 mutations had minor effect on silencing at these regions, they decreased the levels of cohesin on centromeric heterochromatin. Sfh1 also localized at a retrotransposon, Tf2, in a partly Abp1‐dependent manner, and assisted in silencing of Tf2 by Abp1 probably in the same pathway as a histone chaperon, HIRA, which is also known to involve in Tf2 repression. Furthermore, sfh1 mutants were sensitive to several DNA‐damaging treatments (HU, MMS, UV and X‐ray). Increase in spontaneous foci of Rad22, a recombination Mediator protein Rad52 homologue, in sfh1 mutant suggests that RSC functions in homologous recombination repair of double‐stranded break downstream of the Rad22 recruitment. These results indicate that RSC plays multiple roles in the maintenance of genome integrity. We isolated Sfh1, an essential component of chromatin remodeler RSC, as a binding protein of CENP‐B homologue Abp1. Analysis of temperature‐sensitive mutant of Sfh1 showed that Sfh1/RSC involved in double‐strand DNA break repair, cohesin loading at pericetromere and repression of retrotransposons, which shows Sfh1/RSC plays an important role to maintain genome integrity.</abstract><cop>England</cop><pub>Wiley Subscription Services, Inc</pub><pmid>30155942</pmid><doi>10.1111/gtc.12629</doi><tpages>15</tpages><orcidid>https://orcid.org/0000-0002-2023-1303</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1356-9597
ispartof Genes to cells : devoted to molecular & cellular mechanisms, 2018-09, Vol.23 (9), p.738-752
issn 1356-9597
1365-2443
language eng
recordid cdi_proquest_miscellaneous_2096550922
source MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content
subjects Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Centromere
Chromatin Assembly and Disassembly
Chromatin remodeling
Chromosomal Proteins, Non-Histone - genetics
Chromosomal Proteins, Non-Histone - metabolism
Chromosome Segregation
Cohesin
Cohesins
DNA damage
Gene Expression Regulation, Fungal
Genomes
Genomic Instability
Heterochromatin
Homologous recombination
Homologous recombination repair
Mediator protein
Mutation
Rad52 protein
Retroelements
Schizosaccharomyces - genetics
Schizosaccharomyces pombe Proteins - genetics
Schizosaccharomyces pombe Proteins - metabolism
Ultraviolet radiation
Yeast
title Sfh1, an essential component of the RSC chromatin remodeling complex, maintains genome integrity in fission yeast
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-16T07%3A59%3A58IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Sfh1,%20an%20essential%20component%20of%20the%20RSC%20chromatin%20remodeling%20complex,%20maintains%20genome%20integrity%20in%20fission%20yeast&rft.jtitle=Genes%20to%20cells%20:%20devoted%20to%20molecular%20&%20cellular%20mechanisms&rft.au=Kotomura,%20Naoe&rft.date=2018-09&rft.volume=23&rft.issue=9&rft.spage=738&rft.epage=752&rft.pages=738-752&rft.issn=1356-9597&rft.eissn=1365-2443&rft_id=info:doi/10.1111/gtc.12629&rft_dat=%3Cproquest_cross%3E2100368308%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2100368308&rft_id=info:pmid/30155942&rfr_iscdi=true