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Putting the Pieces Together: Histone H2B Ubiquitylation Directly Stimulates Histone H3K79 Methylation
Author(s) -
Jeltsch Albert,
Rathert Philipp
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200800414
Subject(s) - histone methyltransferase , nucleosome , histone methylation , histone code , histone h2b , histone octamer , histone , histone h3 , histone h2a , histone h1 , biochemistry , biology , microbiology and biotechnology , chemistry , dna methylation , dna , gene expression , gene
Employing an in vitro reconstitution approach, McGinty et al. studied the mechanism of stimulation of the Dot1‐catalysed histone H3 methylation at Lys79 by histone H2B ubiquitylation at Lys120. To generate nucleosome particles that carry the ubiquitylation at Lys120, they chemically connected three polypeptides—the main parts of histone H3 and ubiquitin expressed in bacteria and a branched synthetic peptide. Using the semisynthetically produced nucleosome substrates and purified Dot1 enzyme, they showed that Dot1 is directly stimulated by the ubiquitylation, thus ruling out the need for further protein factors to mediate the effect.