A dimeric viral SET domain methyltransferase specific to Lys27 of histone H3 - PubMed (original) (raw)

Comparative Study

doi: 10.1038/nsb898.

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Comparative Study

A dimeric viral SET domain methyltransferase specific to Lys27 of histone H3

Karishma L Manzur et al. Nat Struct Biol. 2003 Mar.

Abstract

Site-specific lysine methylation of histones by SET domains is a hallmark for epigenetic control of gene transcription in eukaryotic organisms. Here we report that a SET domain protein from Paramecium bursaria chlorella virus can specifically di-methylate Lys27 in histone H3, a modification implicated in gene silencing. The solution structure of the viral SET domain reveals a butterfly-shaped head-to-head symmetric dimer different from other known protein methyltransferases. Each subunit consists of a Greek-key antiparallel beta-barrel and a three-stranded open-faced sandwich that mediates the dimer interface. Cofactor S-adenosyl-L-methionine (SAM) binds at the opening of the beta-barrel, and amino acids C-terminal to Lys27 in H3 and in the flexible C-terminal tail of the enzyme confer the specificity of this viral histone methyltransferase.

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