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dc.contributor.authorNoguchi, Chiaki
dc.contributor.authorSingh, Tanu
dc.contributor.authorZiegler, Melissa A.
dc.contributor.authorPeake, Jasmine D.
dc.contributor.authorKhair, Lyne
dc.contributor.authorAza, Ana
dc.contributor.authorNakamura, Toru M.
dc.contributor.authorNoguchi, Eishi
dc.date2022-08-11T08:09:53.000
dc.date.accessioned2022-08-23T16:47:11Z
dc.date.available2022-08-23T16:47:11Z
dc.date.issued2019-04-16
dc.date.submitted2019-06-05
dc.identifier.citation<p>Epigenetics Chromatin. 2019 Apr 16;12(1):24. doi: 10.1186/s13072-019-0271-z. <a href="https://doi.org/10.1186/s13072-019-0271-z">Link to article on publisher's site</a></p>
dc.identifier.issn1756-8935 (Linking)
dc.identifier.doi10.1186/s13072-019-0271-z
dc.identifier.pmid30992049
dc.identifier.urihttp://hdl.handle.net/20.500.14038/41031
dc.description.abstractBACKGROUND: Histone acetylation plays an important role in DNA replication and repair because replicating chromatin is subject to dynamic changes in its structures. However, its precise mechanism remains elusive. In this report, we describe roles of the NuA4 acetyltransferase and histone H4 acetylation in replication fork protection in the fission yeast Schizosaccharomyces pombe. RESULTS: Downregulation of NuA4 subunits renders cells highly sensitive to camptothecin, a compound that induces replication fork breakage. Defects in NuA4 function or mutations in histone H4 acetylation sites lead to impaired recovery of collapsed replication forks and elevated levels of Rad52 DNA repair foci, indicating the role of histone H4 acetylation in DNA replication and fork repair. We also show that Vid21 interacts with the Swi1-Swi3 replication fork protection complex and that Swi1 stabilizes Vid21 and promotes efficient histone H4 acetylation. Furthermore, our genetic analysis demonstrates that loss of Swi1 further sensitizes NuA4 and histone H4 mutant cells to replication fork breakage. CONCLUSION: Considering that Swi1 plays a critical role in replication fork protection, our results indicate that NuA4 and histone H4 acetylation promote repair of broken DNA replication forks.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=30992049&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rightsCopyright © The Author(s) 2019. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectAcetylation
dc.subjectChromatin
dc.subjectDNA replication
dc.subjectHistone H4
dc.subjectMst1
dc.subjectNuA4
dc.subjectReplication fork protection complex
dc.subjectReplication forks
dc.subjectSchizosaccharomyces pombe
dc.subjectSwi1
dc.subjectTimeless
dc.subjectVid21
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectBiochemistry
dc.subjectCells
dc.subjectEnzymes and Coenzymes
dc.subjectFungi
dc.subjectGenetic Phenomena
dc.subjectMolecular Biology
dc.subjectStructural Biology
dc.titleThe NuA4 acetyltransferase and histone H4 acetylation promote replication recovery after topoisomerase I-poisoning
dc.typeJournal Article
dc.source.journaltitleEpigenetics and chromatin
dc.source.volume12
dc.source.issue1
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=4839&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/3825
dc.identifier.contextkey14670814
refterms.dateFOA2022-08-23T16:47:12Z
html.description.abstract<p>BACKGROUND: Histone acetylation plays an important role in DNA replication and repair because replicating chromatin is subject to dynamic changes in its structures. However, its precise mechanism remains elusive. In this report, we describe roles of the NuA4 acetyltransferase and histone H4 acetylation in replication fork protection in the fission yeast Schizosaccharomyces pombe.</p> <p>RESULTS: Downregulation of NuA4 subunits renders cells highly sensitive to camptothecin, a compound that induces replication fork breakage. Defects in NuA4 function or mutations in histone H4 acetylation sites lead to impaired recovery of collapsed replication forks and elevated levels of Rad52 DNA repair foci, indicating the role of histone H4 acetylation in DNA replication and fork repair. We also show that Vid21 interacts with the Swi1-Swi3 replication fork protection complex and that Swi1 stabilizes Vid21 and promotes efficient histone H4 acetylation. Furthermore, our genetic analysis demonstrates that loss of Swi1 further sensitizes NuA4 and histone H4 mutant cells to replication fork breakage.</p> <p>CONCLUSION: Considering that Swi1 plays a critical role in replication fork protection, our results indicate that NuA4 and histone H4 acetylation promote repair of broken DNA replication forks.</p>
dc.identifier.submissionpathoapubs/3825
dc.contributor.departmentDepartment of Surgery
dc.source.pages24


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Copyright © The Author(s) 2019. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
Except where otherwise noted, this item's license is described as Copyright © The Author(s) 2019. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.