Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation

Robert K. McGinty, Jaehoon Kim, Champak Chatterjee, Robert G. Roeder and Tom W. Muir ()
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Robert K. McGinty: Laboratory of Synthetic Protein Chemistry, The Rockefeller University, New York, New York 10065, USA
Jaehoon Kim: Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, New York 10065, USA
Champak Chatterjee: Laboratory of Synthetic Protein Chemistry, The Rockefeller University, New York, New York 10065, USA
Robert G. Roeder: Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, New York 10065, USA
Tom W. Muir: Laboratory of Synthetic Protein Chemistry, The Rockefeller University, New York, New York 10065, USA

Nature, 2008, vol. 453, issue 7196, 812-816

Abstract: Chemical ubiquitylation of histones Previous studies have suggested that histone H2B ubiquitylation and H3 K79 methylation are correlated; however, the underlying mechanism of this crosstalk is not understood, in a large part due to the difficulty of isolating homogenously ubiquitylated H2B (uH2B). McGinty et al. overcame this obstacle by developing a synthetic route to obtain uH2B, employing two traceless chemical ligation strategies. Incorporation of this protein into chemically defined nucleosomes has allowed the demonstration that ubiquitylation of H2B directly stimulates methylation of H3 K79 by the methyltransferase hDot1L in an intranucleosomal fashion.

Date: 2008
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DOI: 10.1038/nature06906

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