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XB-ART-1755
Cell. June 17, 2005; 121 (6): 859-72.

WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development.

Wysocka J , Swigut T , Milne TA , Dou Y , Zhang X , Burlingame AL , Roeder RG , Brivanlou AH , Allis CD .


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.

PubMed ID: 15960974
Article link: Cell.
Grant support: GM 53512 NIGMS NIH HHS , R01 GM066977 NIGMS NIH HHS , RR001614 NCRR NIH HHS , RR015804 NCRR NIH HHS

Genes referenced: hoxc8 kmt2a kmt2b wdr5
Antibodies referenced:
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