CREB-Binding Protein and Histone Deacetylase Regulate the Transcriptional Activity of Kaposi's Sarcoma-Associated Herpesvirus Open Reading Frame 50

• DOI: 10.1128/jvi.75.4.1909-1917.2001
• Publication Date: 2002-07-27T10:06:37Z
• Authors: Yousang Gwack; Hyewon Byun; Seungmin Hwang; Chunghun Lim; Joonho Choe
• Keywords: CREB-binding protein; Transcription; Kaposi's sarcoma-associated herpesvirus; GATAD2B

ABSTRACT Kaposi's sarcoma (KS)-associated herpesvirus (KSHV) open reading frame 50 (ORF50) encodes a viral transcriptional activator, which binds to the KSHV promoter and stimulates transcription of early late genes, thus activating lytic cycle KSHV. We report here that ORF50 cellular proteins CREB-binding protein (CBP) histone deacetylase (HDAC) these binding events modulate ORF50-activated transcription. Binding CBP HDAC activates represses, respectively, ORF50-mediated was shown bind C/H3 domain C-terminal activation CBP, while bound amino-terminal basic carboxyl-terminal transactivation ORF50. The LXXLL motif within is reminiscent CBP-binding sequence found in nuclear receptor proteins. adenovirus E1A protein, also repressed activity c-Jun, kinase-induced ORF50, stimulated HDAC1-interacting be central proline-rich sequence. Our data provide framework for delineating regulatory mechanisms used by its replication through interaction with both acetyltransferases HDACs.