{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T16:00:40Z","timestamp":1781107240552,"version":"3.54.1"},"reference-count":53,"publisher":"National Academy of Sciences","issue":"26","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2000,12,19]]},"abstract":"<jats:p>\n                    Adenovirus E1A mediates its effects on cellular transformation and\n transcription by interacting with critical cellular proteins involved\n in cell growth and differentiation. The amino terminus of E1A binds to\n CBP\/p300 and associated histone acetyltransferases such as P\/CAF.\n The carboxyl terminus binds to the carboxyl-terminal binding protein\n (CtBP), which associates with histone deacetylases. We show that 12S\n E1A can be acetylated by p300 and P\/CAF and map one of the\n acetylation sites to Lys-239. This Lys residue is adjacent to the\n consensus CtBP binding motif, PXDLS. Mutation of Lys-239 to Gln or Ala\n blocks CtBP binding\n                    <jats:italic>in vitro<\/jats:italic>\n                    and disrupts the E1A\u2013CtBP\n interaction\n                    <jats:italic>in vivo<\/jats:italic>\n                    . Peptide competition assays\n demonstrated that the interaction of E1A with CtBP is also blocked by\n Lys-239 acetylation. Supporting a functional role for Lys-239 in CtBP\n binding, mutation of this residue to Ala decreases the ability of E1A\n to block cAMP-regulated enhancer (CRE)-binding protein\n (CREB)-stimulated gene expression. Finally, we demonstrate that Lys-239\n is acetylated in cells by using an antibody directed against an\n acetyl-Lys-239 E1A peptide. CtBP interacts with a wide variety of other\n transcriptional repressors through the PXDLS motif, and, in many\n instances, this motif is followed by a Lys residue. We suggest that\n acetylation of this residue by histone acetyltransferases, and the\n consequent disruption of repressor complexes, might be a general\n mechanism for gene activation.\n                  <\/jats:p>","DOI":"10.1073\/pnas.011283598","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:44:19Z","timestamp":1027680259000},"page":"14323-14328","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":103,"title":["Acetylation of adenovirus E1A regulates binding of the transcriptional corepressor CtBP"],"prefix":"10.1073","volume":"97","author":[{"given":"Qinghong","family":"Zhang","sequence":"first","affiliation":[{"name":"Vollum Institute, Oregon Health Sciences University, Portland, OR\r 97201"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hong","family":"Yao","sequence":"additional","affiliation":[{"name":"Vollum Institute, Oregon Health Sciences University, Portland, OR\r 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