WDR5 Interacts with Mixed Lineage Leukemia (MLL) Protein via the Histone H3-binding Pocket

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WDR5 is a component of the mixed lineage leukemia (MLL) complex, which methylates lysine 4 of histone H3, and was identified as a methylated Lys-4 histone H3-binding protein. Here, we present a crystal structure of WDR5 bound to an MLL peptide. Surprisingly, we find that WDR5 utilizes the same pocket shown to bind histone H3 for this MLL interaction. Furthermore, the WDR5-MLL interaction is disrupted preferentially by mono- and di-methylated Lys-4 histone H3 over unmodified and tri-methylated Lys-4 histone H3. These data implicate a delicate interplay between the effector, WDR5, the catalytic subunit, MLL, and the substrate, histone H3, of the MLL complex. We suggest that the activity of the MLL complex might be regulated through this interplay.
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Issue Date
2008-12
Language
English
Article Type
Article
Keywords

STRUCTURAL BASIS; MOLECULAR RECOGNITION; H3; COMPLEX

Citation

JOURNAL OF BIOLOGICAL CHEMISTRY, v.283, no.50, pp.35258 - 35264

ISSN
0021-9258
DOI
10.1074/jbc.M806900200
URI
http://hdl.handle.net/10203/89951
Appears in Collection
BS-Journal Papers(저널논문)
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