{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,7]],"date-time":"2026-02-07T21:46:08Z","timestamp":1770500768327,"version":"3.49.0"},"reference-count":22,"publisher":"Springer Science and Business Media LLC","issue":"2","license":[{"start":{"date-parts":[[2001,2,1]],"date-time":"2001-02-01T00:00:00Z","timestamp":980985600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["www.embopress.org"],"crossmark-restriction":false},"short-container-title":["EMBO Reports"],"published-print":{"date-parts":[[2001,2]]},"abstract":"<jats:p>\n                    The MCM proteins are essential for the initiation of DNA replication. We have isolated an MCM3\u2010associated protein (MCM3AP) in a two\u2010hybrid screen using MCM3. Here we demonstrate that MCM3AP is an acetyltransferase which acetylates MCM3 and that chromatin\u2010bound MCM3 is acetylated\n                    <jats:italic>in vivo<\/jats:italic>\n                    . The MCM3 acetylase, MCM3AP, is also chromatin\u2010bound. This study also indicates that MCM3AP contains putative acetyl CoA binding motifs conserved within the GCN5\u2010related\n                    <jats:italic>N<\/jats:italic>\n                    \u2010acetyltransferase superfamily. Mutation of those motifs significantly inhibits the MCM3 acetylase activity. Over\u2010expression of MCM3AP inhibits DNA replication, whereas mutation of the acetylase motifs abolishes this effect, suggesting that acetylation plays a role in DNA replication. Taken together, we suggest that MCM3 acetylation is a novel pathway which might regulate DNA replication.\n                  <\/jats:p>","DOI":"10.1093\/embo-reports\/kve026","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T18:50:23Z","timestamp":1027709423000},"page":"119-123","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":73,"title":["MCM3AP, a novel acetyltransferase that acetylates replication protein MCM3"],"prefix":"10.1038","volume":"2","author":[{"given":"Yoshinori","family":"Takei","sequence":"first","affiliation":[{"name":"Wellcome\/CRC Institute  Tennis Court Road Cambridge CB2 1QR UK"},{"name":"Department of Zoology, University of Cambridge  Cambridge CB2 3EJ UK"}]},{"given":"Magdalena","family":"Swietlik","sequence":"additional","affiliation":[{"name":"Wellcome\/CRC Institute  Tennis Court Road Cambridge CB2 1QR UK"},{"name":"Department of Zoology, University of Cambridge  Cambridge CB2 3EJ UK"}]},{"given":"Akito","family":"Tanoue","sequence":"additional","affiliation":[{"name":"Division of Molecular Cell Pharmacology, National Children's Medical Research Center  3\u201035\u201031 Taishido Setagayaku Tokyo 154\u20108509 Japan"}]},{"given":"Gozoh","family":"Tsujimoto","sequence":"additional","affiliation":[{"name":"Division of Molecular Cell Pharmacology, National Children's Medical Research Center  3\u201035\u201031 Taishido Setagayaku Tokyo 154\u20108509 Japan"}]},{"given":"Tony","family":"Kouzarides","sequence":"additional","affiliation":[{"name":"Wellcome\/CRC Institute  Tennis Court Road Cambridge CB2 1QR UK"},{"name":"Department of Pathology, University of Cambridge  Cambridge CB2 1QP UK"}]},{"given":"Ronald","family":"Laskey","sequence":"additional","affiliation":[{"name":"Wellcome\/CRC Institute  Tennis Court Road Cambridge CB2 1QR UK"},{"name":"Department of Zoology, University of Cambridge  Cambridge CB2 3EJ 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