JGV Direct - KSHV K8 interacts with hSNF5 (S. Hwang and others)

								ARTICLE ABSTRACT
								DOI: 10.1099/vir.0.18699-0
								Online 25 November 2002

Kaposi's sarcoma-associated herpesvirus K8 protein interacts with hSNF5

Seungmin Hwang,¹ Daeyoup Lee,¹ Yousang Gwack,¹ Hyesun Min² and Joonho Choe¹

¹Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea
²Department of Food and Nutrition, Hannam University, Daejeon 306-791, Korea

Kaposi's sarcoma-associated herpesvirus (KSHV) is a human gammaherpesvirus related to Epstein–Barr virus (EBV) and herpesvirus saimiri. KSHV open reading frame K8 encodes a basic region-leucine zipper protein of 237 aa that homodimerizes. K8 shows significant similarity to the EBV immediate-early protein Zta, a key regulator of EBV reactivation and replication. In this study, a carboxyl-terminal deletion mutant of K8, K8(1–115), that had strong transactivating properties was found. Screening using transcriptionally inactive K8(1–75) showed that K8 interacts and co-localizes with hSNF5, a cellular chromatin-remodelling factor, both in vivo and in vitro. This interaction requires aa 48–183 of hSNF5 and 1–75 of K8. In a yeast expression system, the ability of K8 and K8(1–115) to activate transcription requires the presence of SNF5, the yeast homologue of hSNF5. These data suggest a mechanism by which the SWI–SNF complex is recruited to specific genes. They also suggest that K8 functions as a transcriptional activator under specific conditions and that its transactivation activity requires its interaction with the cellular chromatin remodelling factor hSNF5.

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This article is now available in the March 2003 print issue of JGV (vol. 84, 665–667). The complete issue of the journal may be seen in electronic form on JGV Online.