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

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


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



Publication Data

June 17, 2005

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM 53512
  • Agency: NIGMS NIH HHS, Id: R01 GM066977
  • Agency: NCRR NIH HHS, Id: RR001614
  • Agency: NCRR NIH HHS, Id: RR015804

Mesh Terms

  • Animals
  • Cell Line
  • Genes, Homeobox
  • Heterotrimeric GTP-Binding Proteins
  • Histone-Lysine N-Methyltransferase
  • Histones
  • Humans
  • Lysine
  • Macromolecular Substances
  • Methylation
  • Microfilament Proteins
  • Nucleosomes
  • Vertebrates
  • Xenopus laevis