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J. Biol. Chem., Vol. 277, Issue 38, 34655-34657, September 20, 2002
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From the Dot1 is a non-SET domain protein that methylates
histone H3 at lysine 79, a surface-exposed residue that lies within the
globular domain. In the context of a nucleosome, H3 lysine 79 is
located in close proximity with lysine 123 of histone H2B, a major site for ubiquitination by Rad6. Here we show that Rad6-mediated
ubiquitination of H2B lysine 123 is important for efficient methylation
of lysine 79, but not lysine 36, of histone H3. In contrast, lysine 79 methylation of H3 is not required for ubiquitination of H2B. Our study
provides a new example of trans-histone regulation between
modifications on different histones. In addition, it suggests that Rad6
affects telomeric silencing, at least in part, by influencing
methylation of histone H3.
ACCELERATED PUBLICATION
Ubiquitination of Histone H2B by Rad6 Is Required for Efficient
Dot1-mediated Methylation of Histone H3 Lysine 79*
,
, and**
Department of Biological Chemistry and
Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts
02115, § W. M. Keck Structural Biology Laboratory, Cold
Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, and
¶ Department of Biochemistry and Biophysics, Lineberger
Comprehensive Cancer Center, University of North Carolina at Chapel
Hill, Chapel Hill, North Carolina 27599
*
This work was supported by a postdoctoral fellowship from
the Cancer Research Fund of the Damon Runyon Walter Winchell Foundation (to H. H. N.) and National Institutes of Health Grants GM53720 (to
K. S.) and GM63067 (to Y. Z.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
A Kimmel Scholar and also supported by American Cancer Society
Grant RSG-00-351-01-GMC.
**
To whom correspondence should be addressed. Tel.: 617-432-2104;
E-mail: kevin@hms.harvard.edu.
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