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dc.contributor.authorXie, Jenny X.
dc.contributor.authorPeng, Min
dc.contributor.authorGuillemette, Shawna
dc.contributor.authorQuan, Steven
dc.contributor.authorManiatis, Stephanie
dc.contributor.authorWu, Yuliang
dc.contributor.authorVenkatesh, Aditya
dc.contributor.authorShaffer, Scott A.
dc.contributor.authorBrosh, Robert M. Jr.
dc.contributor.authorCantor, Sharon B.
dc.date2022-08-11T08:09:40.000
dc.date.accessioned2022-08-23T16:39:44Z
dc.date.available2022-08-23T16:39:44Z
dc.date.issued2012-07-05
dc.date.submitted2012-09-06
dc.identifier.citationXie J, Peng M, Guillemette S, Quan S, Maniatis S, et al. (2012) FANCJ/BACH1 Acetylation at Lysine 1249 Regulates the DNA Damage Response. PLoS Genet 8(7): e1002786. doi:10.1371/journal.pgen.1002786. <a href="http://dx.doi.org/10.1371/journal.pgen.1002786" target="_blank">Link to article on publisher's site</a>
dc.identifier.issn1553-7390 (Linking)
dc.identifier.doi10.1371/journal.pgen.1002786
dc.identifier.pmid22792074
dc.identifier.urihttp://hdl.handle.net/20.500.14038/39538
dc.description.abstractBRCA1 promotes DNA repair through interactions with multiple proteins, including CtIP and FANCJ (also known as BRIP1/BACH1). While CtIP facilitates DNA end resection when de-acetylated, the function of FANCJ in repair processing is less well defined. Here, we report that FANCJ is also acetylated. Preventing FANCJ acetylation at lysine 1249 does not interfere with the ability of cells to survive DNA interstrand crosslinks (ICLs). However, resistance is achieved with reduced reliance on recombination. Mechanistically, FANCJ acetylation facilitates DNA end processing required for repair and checkpoint signaling. This conclusion was based on the finding that FANCJ and its acetylation were required for robust RPA foci formation, RPA phosphorylation, and Rad51 foci formation in response to camptothecin (CPT). Furthermore, both preventing and mimicking FANCJ acetylation at lysine 1249 disrupts FANCJ function in checkpoint maintenance. Thus, we propose that the dynamic regulation of FANCJ acetylation is critical for robust DNA damage response, recombination-based processing, and ultimately checkpoint maintenance.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=22792074&dopt=Abstract">Link to Article in PubMed</a>
dc.rights<p>Copyright: © 2012 Cantor et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.</p>
dc.subjectAcetylation
dc.subjectBasic-Leucine Zipper Transcription Factors
dc.subjectDNA
dc.subjectDNA Damage
dc.subjectFanconi Anemia Complementation Group Proteins
dc.subjectLysine
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectCancer Biology
dc.subjectGenetics and Genomics
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleFANCJ/BACH1 Acetylation at Lysine 1249 Regulates the DNA Damage Response
dc.typeJournal Article
dc.source.journaltitlePLoS genetics
dc.source.volume8
dc.source.issue7
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=3332&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/2332
dc.identifier.contextkey3299918
refterms.dateFOA2022-08-23T16:39:45Z
html.description.abstract<p>BRCA1 promotes DNA repair through interactions with multiple proteins, including CtIP and FANCJ (also known as BRIP1/BACH1). While CtIP facilitates DNA end resection when de-acetylated, the function of FANCJ in repair processing is less well defined. Here, we report that FANCJ is also acetylated. Preventing FANCJ acetylation at lysine 1249 does not interfere with the ability of cells to survive DNA interstrand crosslinks (ICLs). However, resistance is achieved with reduced reliance on recombination. Mechanistically, FANCJ acetylation facilitates DNA end processing required for repair and checkpoint signaling. This conclusion was based on the finding that FANCJ and its acetylation were required for robust RPA foci formation, RPA phosphorylation, and Rad51 foci formation in response to camptothecin (CPT). Furthermore, both preventing and mimicking FANCJ acetylation at lysine 1249 disrupts FANCJ function in checkpoint maintenance. Thus, we propose that the dynamic regulation of FANCJ acetylation is critical for robust DNA damage response, recombination-based processing, and ultimately checkpoint maintenance.</p>
dc.identifier.submissionpathoapubs/2332
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.contributor.departmentDepartment of Cancer Biology
dc.source.pagese1002786


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