The human HELLS chromatin remodelling protein promotes end resection to facilitate homologous recombination and contributes to DSB repair within heterochromatin
Identifieur interne : 000C81 ( Ncbi/Merge ); précédent : 000C80; suivant : 000C82The human HELLS chromatin remodelling protein promotes end resection to facilitate homologous recombination and contributes to DSB repair within heterochromatin
Auteurs : Gabriel Kollárovi ; Caitríona E. Topping ; Edward P. Shaw ; Anna L. ChambersSource :
- Nucleic Acids Research [ 0305-1048 ] ; 2019.
Abstract
Efficient double-strand break repair in eukaryotes requires manipulation of chromatin structure. ATP-dependent chromatin remodelling enzymes facilitate different DNA repair pathways, during different stages of the cell cycle and in varied chromatin environments. The contribution of remodelling factors to double-strand break repair within heterochromatin during G2 is unclear. The human HELLS protein is a Snf2-like chromatin remodeller family member and is mutated or misregulated in several cancers and some cases of ICF syndrome. HELLS has been implicated in the DNA damage response, but its mechanistic function in repair is not well understood. We discover that HELLS facilitates homologous recombination at two-ended breaks and contributes to repair within heterochromatic regions during G2. HELLS promotes initiation of HR by facilitating end-resection and accumulation of CtIP at IR-induced foci. We identify an interaction between HELLS and CtIP and establish that the ATPase domain of HELLS is required to promote DSB repair. This function of HELLS in maintenance of genome stability is likely to contribute to its role in cancer biology and demonstrates that different chromatin remodelling activities are required for efficient repair in specific genomic contexts.
Url:
DOI: 10.1093/nar/gkz1146
PubMed: 31802118
PubMed Central: 7038987
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Topping</name><affiliation><nlm:aff id="AFF1"></nlm:aff></affiliation></author><author><name sortKey="Shaw, Edward P" sort="Shaw, Edward P" uniqKey="Shaw E" first="Edward P" last="Shaw">Edward P. Shaw</name><affiliation><nlm:aff id="AFF1"></nlm:aff></affiliation></author><author><name sortKey="Chambers, Anna L" sort="Chambers, Anna L" uniqKey="Chambers A" first="Anna L" last="Chambers">Anna L. Chambers</name><affiliation><nlm:aff id="AFF1"></nlm:aff></affiliation></author></analytic><series><title level="j">Nucleic Acids Research</title><idno type="ISSN">0305-1048</idno><idno type="eISSN">1362-4962</idno><imprint><date when="2019">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Abstract</title><p>Efficient double-strand break repair in eukaryotes requires manipulation of chromatin structure. ATP-dependent chromatin remodelling enzymes facilitate different DNA repair pathways, during different stages of the cell cycle and in varied chromatin environments. The contribution of remodelling factors to double-strand break repair within heterochromatin during G2 is unclear. The human HELLS protein is a Snf2-like chromatin remodeller family member and is mutated or misregulated in several cancers and some cases of ICF syndrome. HELLS has been implicated in the DNA damage response, but its mechanistic function in repair is not well understood. We discover that HELLS facilitates homologous recombination at two-ended breaks and contributes to repair within heterochromatic regions during G2. HELLS promotes initiation of HR by facilitating end-resection and accumulation of CtIP at IR-induced foci. We identify an interaction between HELLS and CtIP and establish that the ATPase domain of HELLS is required to promote DSB repair. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Nucleic Acids Res</journal-id><journal-id journal-id-type="iso-abbrev">Nucleic Acids Res</journal-id><journal-id journal-id-type="publisher-id">nar</journal-id><journal-title-group><journal-title>Nucleic Acids Research</journal-title></journal-title-group><issn pub-type="ppub">0305-1048</issn><issn pub-type="epub">1362-4962</issn><publisher><publisher-name>Oxford University Press</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">31802118</article-id><article-id pub-id-type="pmc">7038987</article-id><article-id pub-id-type="doi">10.1093/nar/gkz1146</article-id><article-id pub-id-type="publisher-id">gkz1146</article-id><article-categories><subj-group subj-group-type="heading"><subject>Genome Integrity, Repair and Replication</subject></subj-group></article-categories><title-group><article-title>The human HELLS chromatin remodelling protein promotes end resection to facilitate homologous recombination and contributes to DSB repair within heterochromatin</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Kollárovič</surname><given-names>Gabriel</given-names></name><xref ref-type="aff" rid="AFF1"></xref></contrib><contrib contrib-type="author"><name><surname>Topping</surname><given-names>Caitríona E</given-names></name><xref ref-type="aff" rid="AFF1"></xref></contrib><contrib contrib-type="author"><name><surname>Shaw</surname><given-names>Edward P</given-names></name><xref ref-type="aff" rid="AFF1"></xref></contrib><contrib contrib-type="author"><contrib-id contrib-id-type="orcid" authenticated="false">http://orcid.org/0000-0001-8133-6240</contrib-id><name><surname>Chambers</surname><given-names>Anna L</given-names></name><pmc-comment>a.chambers@bristol.ac.uk </pmc-comment>
<xref ref-type="corresp" rid="COR1"></xref><xref ref-type="aff" rid="AFF1"></xref></contrib></contrib-group><aff id="AFF1"><institution>DNA-protein Interactions Unit, School of Biochemistry, University of Bristol</institution>, Bristol BS8 1TD,<country country="GB">UK</country></aff><author-notes><corresp id="COR1">To whom correspondence should be addressed. Tel: +44 117 3311622; Email: <email>a.chambers@bristol.ac.uk</email></corresp></author-notes><pub-date pub-type="ppub"><day>28</day><month>2</month><year>2020</year></pub-date><pub-date pub-type="epub" iso-8601-date="2019-12-05"><day>05</day><month>12</month><year>2019</year></pub-date><pub-date pub-type="pmc-release"><day>05</day><month>12</month><year>2019</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
<volume>48</volume><issue>4</issue><fpage>1872</fpage><lpage>1885</lpage><history><date date-type="accepted"><day>22</day><month>11</month><year>2019</year></date><date date-type="rev-recd"><day>18</day><month>11</month><year>2019</year></date><date date-type="received"><day>21</day><month>5</month><year>2019</year></date></history><permissions><copyright-statement>© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.</copyright-statement><copyright-year>2019</copyright-year><license license-type="cc-by" xlink:href="http://creativecommons.org/licenses/by/4.0/"><license-p>This is an Open Access article distributed under the terms of the Creative Commons Attribution License (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/4.0/">http://creativecommons.org/licenses/by/4.0/</ext-link>), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.</license-p></license></permissions><self-uri xlink:href="gkz1146.pdf"></self-uri><abstract><title>Abstract</title><p>Efficient double-strand break repair in eukaryotes requires manipulation of chromatin structure. ATP-dependent chromatin remodelling enzymes facilitate different DNA repair pathways, during different stages of the cell cycle and in varied chromatin environments. The contribution of remodelling factors to double-strand break repair within heterochromatin during G2 is unclear. The human HELLS protein is a Snf2-like chromatin remodeller family member and is mutated or misregulated in several cancers and some cases of ICF syndrome. HELLS has been implicated in the DNA damage response, but its mechanistic function in repair is not well understood. We discover that HELLS facilitates homologous recombination at two-ended breaks and contributes to repair within heterochromatic regions during G2. HELLS promotes initiation of HR by facilitating end-resection and accumulation of CtIP at IR-induced foci. We identify an interaction between HELLS and CtIP and establish that the ATPase domain of HELLS is required to promote DSB repair. This function of HELLS in maintenance of genome stability is likely to contribute to its role in cancer biology and demonstrates that different chromatin remodelling activities are required for efficient repair in specific genomic contexts.</p></abstract><funding-group><award-group award-type="grant"><funding-source><named-content content-type="funder-name">Cancer Research UK</named-content><named-content content-type="funder-identifier">10.13039/501100000289</named-content></funding-source><award-id>C49963/A1750</award-id></award-group></funding-group><counts><page-count count="14"></page-count></counts></article-meta></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Chambers, Anna L" sort="Chambers, Anna L" uniqKey="Chambers A" first="Anna L" last="Chambers">Anna L. Chambers</name><name sortKey="Kollarovi, Gabriel" sort="Kollarovi, Gabriel" uniqKey="Kollarovi G" first="Gabriel" last="Kollárovi">Gabriel Kollárovi</name><name sortKey="Shaw, Edward P" sort="Shaw, Edward P" uniqKey="Shaw E" first="Edward P" last="Shaw">Edward P. Shaw</name><name sortKey="Topping, Caitriona E" sort="Topping, Caitriona E" uniqKey="Topping C" first="Caitríona E" last="Topping">Caitríona E. Topping</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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