Journal
EPIGENETICS
Volume 5, Issue 6, Pages -Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/epi.5.6.12314
Keywords
chromatin; H2B ubiquitination; H3K4 methylation; H3K79 methylation; nucleosome stability; trans-histone
Funding
- The Vanderbilt-Ingram Cancer Center
- The Robert J. and Helen C. Kleberg Foundation
- NCI SPORE in Breast Cancer [5P0CA098131]
- National Institutes of Heath [RO1CA109355]
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Regulation of Set1-COMPASS-mediated H3K4 methylation and Dot1-mediated H3K79 methylation by H2BK123 ubiquitination (H2Bub1) is an evolutionarily conserved trans-histone crosstalk mechanism. How H2Bub1 impacts chromatin structure and affects Set1-COMPASS/Dot1 functions has not been fully defined. Ubiquitin was proposed to bind proteins to physically bridge H2Bub1 with Set1-COMPASS/Dot1. Alternatively, the bulky ubiquitin was thought to be a wedge that loosens the nucleosome for factor access. Contrary to the latter possibility, recent discoveries provide evidence for nucleosome stabilization by H2Bub1 via preventing the constant H2A-H2B eviction. Recent data has also uncovered a docking-site on H2B for Set1-COMPASS. Collectively, these findings invoke a model, where ubiquitin acts as a glue to bind the nucleosome together for supporting Set1-COMPASS/Dot1 functions. This review provides an overview of these novel findings. Additionally, how H2Bub1 and its deubiquitination might alter the chromatin dynamics during transcription is discussed. Possible models for nucleosome stabilization by ubiquitin are also provided.
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