{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T06:31:00Z","timestamp":1791268260339,"version":"4.1.0"},"reference-count":57,"publisher":"American Society for Microbiology","issue":"21","license":[{"start":{"date-parts":[[2006,11,1]],"date-time":"2006-11-01T00:00:00Z","timestamp":1162339200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2006,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The Kaposi's sarcoma-associated herpesvirus (KSHV) latency-associated\nnuclear antigen 1 (LANA-1) is required for the replication of episomal\nviral genomes. Regions in its N-terminal and C-terminal domains mediate\nthe interaction with host cell chromatin. Several cellular nuclear\nproteins, e.g., BRD2\/RING3, histones H2A and H2B, MeCP2, DEK, and\nHP1\u03b1, have been suggested to mediate this interaction. In this\nwork, we identify the double-bromodomain proteins BRD4 and BRD3\/ORFX as\nadditional LANA-1 interaction partners. The carboxy-terminal region of\nthe short variant of BRD4 (BRD4\n            <jats:sup>S<\/jats:sup>\n            ) containing the highly\nconserved extraterminal domain directly interacts with an element in\nthe LANA-1 carboxy-terminal domain. We show that ectopically expressed\nBRD4\n            <jats:sup>S<\/jats:sup>\n            and BRD2\/RING3 delay progression into the S phase of\nthe cell cycle in epithelial and B-cell lines and increase cyclin E\npromoter activity. LANA-1 partly releases epithelial and B cells from a\nBRD4\n            <jats:sup>S<\/jats:sup>\n            - and BRD2\/RING3-induced G\n            <jats:sub>1<\/jats:sub>\n            cell cycle\narrest and also promotes S-phase entry in the presence of\nBRD4\n            <jats:sup>S<\/jats:sup>\n            and BRD2\/RING3. This is accompanied by a reduction in\nBRD4\n            <jats:sup>S<\/jats:sup>\n            -mediated cyclin E promoter activity. Our data are in\nkeeping with the notion that the direct interaction of KSHV LANA-1 with\nBRD4 and other BRD proteins could play a role in the G\n            <jats:sub>1<\/jats:sub>\n            \/S\nphase-promoting functions of KSHV LANA-1. Further, our data support a\nmodel in which the LANA-1 C terminus contributes to a functional\nattachment to acetylated histones H3 and H4 via BRD4 and BRD2, in\naddition to the recently demonstrated direct interaction (A. \nJ. Barbera, J. V. Chodaparambil, B. Kelley-Clarke, V. Joukov,\nJ. C. Walter, K. Luger, and K. M. Kaye, Science\n311:856-861, 2006) of the LANA-1 N terminus with histones H2A\nand\nH2B.\n          <\/jats:p>","DOI":"10.1128\/jvi.00804-06","type":"journal-article","created":{"date-parts":[[2006,10,15]],"date-time":"2006-10-15T06:42:36Z","timestamp":1160894556000},"page":"10772-10786","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":136,"title":["Kaposi's Sarcoma-Associated Herpesvirus LANA-1 Interacts with the Short Variant of BRD4 and Releases Cells from a BRD4- and BRD2\/RING3-Induced G\n            <sub>1<\/sub>\n            Cell CycleArrest"],"prefix":"10.1128","volume":"80","author":[{"given":"Matthias","family":"Ottinger","sequence":"first","affiliation":[{"name":"Institut fu\u0308r Virologie, Medizinische Hochschule Hannover, Carl-Neuberg\rStr. 1, D-30625 Hannover, Germany"},{"name":"Department of Pathology, Harvard Medical School, Boston,\rMassachusetts"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Christalla","sequence":"additional","affiliation":[{"name":"Institut fu\u0308r Virologie, Medizinische Hochschule Hannover, Carl-Neuberg\rStr. 1, D-30625 Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kavita","family":"Nathan","sequence":"additional","affiliation":[{"name":"Institut fu\u0308r Virologie, Medizinische Hochschule Hannover, Carl-Neuberg\rStr. 1, D-30625 Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Melanie M.","family":"Brinkmann","sequence":"additional","affiliation":[{"name":"Institut fu\u0308r Virologie, Medizinische Hochschule Hannover, Carl-Neuberg\rStr. 1, D-30625 Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abel","family":"Viejo-Borbolla","sequence":"additional","affiliation":[{"name":"Institut fu\u0308r Virologie, Medizinische Hochschule Hannover, Carl-Neuberg\rStr. 1, D-30625 Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas F.","family":"Schulz","sequence":"additional","affiliation":[{"name":"Institut fu\u0308r Virologie, Medizinische Hochschule Hannover, Carl-Neuberg\rStr. 1, D-30625 Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M407435200"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.78.1.294-301.2004"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1120541"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.77.11.6474-6481.2003"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM199505043321802"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.7997879"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.15.7.3685"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1021\/pr050430u"},{"key":"e_1_3_2_10_2","first-page":"417","volume":"11","year":"2000","unstructured":"Denis, G. 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