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In <jats:styled-content style=\"fixed-case\">EBV<\/jats:styled-content>, the product of the <jats:italic><jats:styled-content style=\"fixed-case\">BZLF<\/jats:styled-content>1<\/jats:italic> gene (<jats:styled-content style=\"fixed-case\">ZEBRA<\/jats:styled-content>) acts as a master regulator of the transition from latency to the lytic replication cycle in latently infected cells. <jats:styled-content style=\"fixed-case\">EBV<\/jats:styled-content> latency is primarily maintained by hypoacetylation of histone proteins in the <jats:italic><jats:styled-content style=\"fixed-case\">BZLF<\/jats:styled-content>1<\/jats:italic> promoter by histone deacetylases. Although histone methylation is involved in the organization of chromatin domains and has a central epigenetic role in gene expression, its role in maintaining <jats:styled-content style=\"fixed-case\">EBV<\/jats:styled-content> latency is not well understood. Here we present evidence that the histone H3 lysine\u00a09 (H3K9) methyltransferase suppressor of variegation 3\u20139 homolog\u00a01 (Suv39\u00a0h1) transcriptionally represses <jats:italic><jats:styled-content style=\"fixed-case\">BZLF<\/jats:styled-content>1<\/jats:italic> in B95\u20138 cells by promoting repressive trimethylation at H3K9 (H3K9me3). Suv39\u00a0h1 significantly inhibited basal expression and <jats:styled-content style=\"fixed-case\">ZEBRA<\/jats:styled-content>\u2010induced <jats:italic><jats:styled-content style=\"fixed-case\">BZLF<\/jats:styled-content>1<\/jats:italic> gene expression in B95\u20138 B cells. However, mutant Suv39\u00a0h1 lacks the <jats:styled-content style=\"fixed-case\">SET<\/jats:styled-content> domain responsible for catalytic activity of histone methyl transferase and thus had no such effect. <jats:italic><jats:styled-content style=\"fixed-case\">BZLF<\/jats:styled-content>1<\/jats:italic> transcription was augmented when Suv39\u00a0h1 expression was knocked down by si<jats:styled-content style=\"fixed-case\">RNA<\/jats:styled-content> in B95\u20138 cells, but not in Akata or Raji cells. In addition, treatment with a specific Suv39\u00a0h1 inhibitor, chaetocin, significantly enhanced <jats:italic><jats:styled-content style=\"fixed-case\">BZLF<\/jats:styled-content>1<\/jats:italic> transcription. Furthermore, chromatin immunoprecipitation assays revealed the presence of Suv39\u00a0h1 and H3K9me3 on nucleosome histones near the <jats:italic><jats:styled-content style=\"fixed-case\">BZLF<\/jats:styled-content>1<\/jats:italic> promoter. Taken together, these results suggest that Suv39\u00a0h1\u2013H3K9me3 epigenetic repression is involved in <jats:italic><jats:styled-content style=\"fixed-case\">BZLF<\/jats:styled-content>1<\/jats:italic> transcriptional silencing, providing a molecular basis for understanding the mechanism by which <jats:styled-content style=\"fixed-case\">EBV<\/jats:styled-content> latency is maintained.<\/jats:p>","DOI":"10.1111\/febs.12768","type":"journal-article","created":{"date-parts":[[2014,3,4]],"date-time":"2014-03-04T12:54:37Z","timestamp":1393937677000},"page":"2148-2158","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":31,"title":["Role of the histone <scp>H<\/scp>3 lysine\u00a09 methyltransferase <scp>S<\/scp>uv39\u00a0h1 in maintaining <scp>E<\/scp>psteinn\u2013<scp>B<\/scp>arr virus latency in <scp>B<\/scp>95\u20138 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