Trans-histone regulatory pathway in chromatin

Scott D. Briggs, Tiaojiang Xiao, Zu-Wen Sun, Jennifer A. Caldwell, Jeffrey Shabanowitz, Donald F. Hunt, C. David Allis and Brian D. Strahl ()
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Scott D. Briggs: University of Virginia Health System
Tiaojiang Xiao: University of North Carolina at Chapel Hill
Zu-Wen Sun: University of Virginia Health System
Jennifer A. Caldwell: University of Virginia
Jeffrey Shabanowitz: University of Virginia
Donald F. Hunt: University of Virginia
C. David Allis: University of Virginia Health System
Brian D. Strahl: University of North Carolina at Chapel Hill

Nature, 2002, vol. 418, issue 6897, 498-498

Abstract: Abstract The fundamental unit of eukaryotic chromatin, the nucleosome, consists of genomic DNA wrapped around the conserved histone proteins H3, H2B, H2A and H4, all of which are variously modified at their amino- and carboxy-terminal tails to influence the dynamics of chromatin structure and function1,2 — for example, conjugation of histone H2B with ubiquitin controls the outcome of methylation at a specific lysine residue (Lys 4) on histone H3, which regulates gene silencing in the yeast Saccharomyces cerevisiae3. Here we show that ubiquitination of H2B is also necessary for the methylation of Lys 79 in H3, the only modification known to occur away from the histone tails, but that not all methylated lysines in H3 are regulated by this 'trans-histone' pathway because the methylation of Lys 36 in H3 is unaffected. Given that gene silencing is regulated by the methylation of Lys 4 and Lys 79 in histone H3, we suggest that H2B ubiquitination acts as a master switch that controls the site-selective histone methylation patterns responsible for this silencing.

Date: 2002
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DOI: 10.1038/nature00970

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