| Literature DB >> 15960974 |
Joanna Wysocka1, Tomek Swigut, Thomas A Milne, Yali Dou, Xin Zhang, Alma L Burlingame, Robert G Roeder, Ali H Brivanlou, C David Allis.
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 HOX gene activation in human cells. WDR5 is essential for vertebrate development, in that WDR5-depleted X. laevis tadpoles exhibit a variety of developmental defects and abnormal spatial Hox gene expression. Our results are the first demonstration that a WD40-repeat protein acts as a module for recognition of a specific histone modification and suggest a mechanism for reading and writing an epigenetic mark for gene activation.Entities:
Mesh：
Substances：
Year: 2005 PMID： 15960974 DOI： 10.1016/j.cell.2005.03.036
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582