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However, little is known as to how PNKP functions in such diverse repair processes. Here we report that PNKP is acetylated at K142 (AcK142) by p300 constitutively but at K226 (AcK226) by CBP, only after DSB induction. Co-immunoprecipitation analysis using AcK142 or AcK226 PNKP-specific antibodies showed that AcK142-PNKP associates only with BER\/SSBR, and AcK226 PNKP with DSBR proteins. Despite the modest effect of acetylation on PNKP\u2019s enzymatic activity in vitro, cells expressing non-acetylable PNKP (K142R or K226R) accumulated DNA damage in transcribed genes. Intriguingly, in striatal neuronal cells of a Huntington's Disease (HD)-based mouse model, K142, but not K226, was acetylated. This is consistent with the reported degradation of CBP, but not p300, in HD cells. Moreover, transcribed genomes of HD cells progressively accumulated DSBs. Chromatin-immunoprecipitation analysis demonstrated the association of Ac-PNKP with the transcribed genes, consistent with PNKP\u2019s role in transcription-coupled repair. Thus, our findings demonstrate that acetylation at two lysine residues, located in different domains of PNKP, regulates its distinct role in BER\/SSBR versus DSBR.<\/jats:p>","DOI":"10.1093\/nar\/gkae002","type":"journal-article","created":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T16:32:43Z","timestamp":1704126763000},"page":"2416-2433","source":"Crossref","is-referenced-by-count":11,"title":["Site-specific acetylation of polynucleotide kinase 3\u2032-phosphatase regulates its distinct role in DNA repair pathways"],"prefix":"10.1093","volume":"52","author":[{"given":"Azharul","family":"Islam","sequence":"first","affiliation":[{"name":"Department of Internal Medicine, University of Texas Medical Branch , Galveston , TX 77555 ,\u00a0 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anirban","family":"Chakraborty","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine, University of Texas Medical Branch , Galveston , TX 77555 ,\u00a0 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Altaf H","family":"Sarker","sequence":"additional","affiliation":[{"name":"Life Sciences Division, Lawrence Berkeley National Laboratory , Berkeley , CA 94720 ,\u00a0 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Uma K","family":"Aryal","sequence":"additional","affiliation":[{"name":"Purdue Proteomics Facility, Bindley Bioscience Center, Purdue University , IN 47907 ,\u00a0 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lang","family":"Pan","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, University of Texas Medical Branch , Galveston , TX 77555 ,\u00a0 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gulshan","family":"Sharma","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine, University of Texas Medical Branch , Galveston , TX 77555 ,\u00a0 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Istvan","family":"Boldogh","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, University of Texas Medical Branch , Galveston , TX 77555 ,\u00a0 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4587-687X","authenticated-orcid":false,"given":"Tapas","family":"Hazra","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine, University of Texas Medical Branch , Galveston , TX 77555 ,\u00a0 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2024,1,15]]},"reference":[{"key":"2024032102100635400_B1","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1038\/nrc3399","article-title":"DNA repair dysregulation from cancer driver to therapeutic target","volume":"12","author":"Curtin","year":"2012","journal-title":"Nat. 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Mutagen."},{"key":"2024032102100635400_B5","doi-asserted-by":"crossref","first-page":"1193","DOI":"10.1002\/j.1460-2075.1996.tb00458.x","article-title":"Phosphorylation of Okazaki-like DNA fragments in mammalian cells and role of polyamines in the processing of this DNA","volume":"15","author":"Pohjanpelto","year":"1996","journal-title":"EMBO J."},{"key":"2024032102100635400_B6","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0079-6603(01)68095-4","article-title":"Molecular mechanism of PCNA-dependent base excision repair","volume":"68","author":"Matsumoto","year":"2001","journal-title":"Prog. Nucleic Acid Res. Mol. Biol."},{"key":"2024032102100635400_B7","doi-asserted-by":"crossref","first-page":"9573","DOI":"10.1074\/jbc.271.16.9573","article-title":"Two pathways for base excision repair in mammalian cells","volume":"271","author":"Frosina","year":"1996","journal-title":"J. Biol. 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Mol. Genet."},{"key":"2024032102100635400_B27","doi-asserted-by":"crossref","first-page":"104714","DOI":"10.1016\/j.jbc.2023.104714","article-title":"Functional analysis of a conserved site mutation in the DNA end processing enzyme PNKP leading to ataxia with oculomotor apraxia type 4 in humans","volume":"299","author":"Islam","year":"2023","journal-title":"J. Biol. 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