- Abstract:
-
Histone H3 lysine 4 (K4) methylation has been linked to the transcriptional activation in a variety of eukaryotic species. Here we show that a common component of MLL1, MLL2, and hSet1 H3 K4 methyltransferase complexes, the WD40-repeat protein WDR5, directly associates with histone H3 di- and trimethylated at K4 and with H3-K4-dimethylated nucleosomes. WDR5 is required for binding of the methyltransferase complex to the K4-dimethylated H3 tail as well as for global H3 K4 trimethylation and HO...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/j.cell.2005.03.036
-
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- Journal:
- Cell
- Volume:
- 121
- Issue:
- 6
- Pages:
- 859-872
- Publication date:
- 2005-06-05
- DOI:
- EISSN:
-
1097-4172
- ISSN:
-
0092-8674
- URN:
-
uuid:c441e40a-d744-4b5b-bf2e-608d24693bc3
- Source identifiers:
-
331902
- Local pid:
- pubs:331902
- Copyright date:
- 2005
Journal article
WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development.
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