期刊
MOLECULAR CELL
卷 49, 期 6, 页码 1121-1133出版社
CELL PRESS
DOI: 10.1016/j.molcel.2013.01.034
关键词
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资金
- NIH [CA129325, DK071900, CA148354, GM40922]
- Leukemia and Lymphoma Society SCOR grant
- Starr Foundation Cancer Consortium grant
- Basic Science Research Program of the National Research Foundation of Korea (NRF)
- Ministry of Education, Science, and Technology [2012R1A1A1014697, 2012M3A9B4027956, 2012M3A9C6049938]
- TJ Park Junior Faculty Fellowship
- National Research Foundation of Korea [2012M3A9C6049938, 2012R1A1A1014697, 2012M3A9B4027956] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Past studies have documented a crosstalk between H2B ubiquitylation (H2Bub) and H3K4 methylation, but little (if any) direct evidence exists explaining the mechanism underlying H2Bub-dependent H3K4 methylation on chromatin templates. Here, we took advantage of an in vitro histone methyltransferase assay employing a reconstituted yeast Set1 complex (ySet1C) and a recombinant chromatin template containing fully ubiquitylated H2B to gain valuable insights. Combined with genetic analyses, we demonstrate that the n-SET domain within Set1, but not Swd2, is essential for H2Bub-dependent H3K4 methylation. Spp1, a homolog of human CFP1, is conditionally involved in this crosstalk. Our findings extend to the human Set1 complex, underscoring the conserved nature of this disease-relevant crosstalk pathway. As not all members of the H3K4 methyltransferase family contain n-SET domains, our studies draw attention to the n-SET domain as a predictor of an H2B ubiquitylation-sensing mechanism that leads to downstream H3K4 methylation.
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