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Trans-histone regulatory pathway in chromatin

Author

Listed:
  • 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)

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.

Suggested Citation

  • Scott D. Briggs & Tiaojiang Xiao & Zu-Wen Sun & Jennifer A. Caldwell & Jeffrey Shabanowitz & Donald F. Hunt & C. David Allis & Brian D. Strahl, 2002. "Trans-histone regulatory pathway in chromatin," Nature, Nature, vol. 418(6897), pages 498-498, August.
    • Handle: RePEc:nat:nature:v:418:y:2002:i:6897:d:10.1038_nature00970
    DOI: 10.1038/nature00970
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    Cited by:

    1. Shuhei Onishi & Kotone Uchiyama & Ko Sato & Chikako Okada & Shunsuke Kobayashi & Keisuke Hamada & Tomohiro Nishizawa & Osamu Nureki & Kazuhiro Ogata & Toru Sengoku, 2024. "Structure of the human Bre1 complex bound to the nucleosome," Nature Communications, Nature, vol. 15(1), pages 1-11, December.

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