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| Cell Dec (2007); 131(6):1084-96 | |
| Histone crosstalk between H2B monoubiquitination and H3 methylation mediated by COMPASS- | |
| Lee JS, Shukla A, Schneider J, Swanson SK, Washburn MP, Florens L, Bhaumik SR, Shilatifard A | |
| Stowers Institute for Medical Research, 1000 East 50-th- Street, Kansas City, MO 64110, USA- | |
| Abstract: COMPASS, the yeast homolog of the mammalian MLL complex, is a histone H3 lysine 4 -H3K4- methylase consisting of Set1 -KMT2- and seven other polypeptides, including Cps35, the only essential subunit- Histone H2B monoubiquitination by Rad6-Bre1 is required for both H3K4 methylation by COMPASS, and H3K79 methylation by Dot1- However, the molecular mechanism for such histone crosstalk is poorly understood- Here, we demonstrate that histone H2B monoubiquitination controls the binding of Cps35 with COMPASS complex- Cps 35 is required for COMPASS' catalytic activity in vivo, and the addition of exogenous purified Cps35 to COMPASS purified from a Deltarad6 background results in the generation of a methylation competent COMPASS- Cps35 associates with the chromatin of COMPASS-regulated genes in a H2BK123 monoubiquitination-dependent but Set1-independent manner- Cps35 is also required for proper H3K79 trimethylation- These findings offer insight into the molecular role of Cps35 in translating the H2B monoubiquitination signal into H3 methylation- | |
| [PUBMED: 18083099] |   |
| Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |