5ov3
Structure of the RbBP5 beta-propeller domain
Structural highlights
FunctionRBBP5_MOUSE As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid. Does not affect ES cell self-renewal. Publication Abstract from PubMedThe multi-protein complex WRAD, formed by WDR5, RbBP5, Ash2L and Dpy30, binds to the MLL SET domain to stabilize the catalytically active conformation required for histone H3K4 methylation. In addition, the WRAD complex contributes to the targeting of the activated complex to specific sites on chromatin. RbBP5 is central to MLL catalytic activation, by making critical contacts with the other members of the complex. Interestingly its only major structural domain, a canonical WD40 repeat beta-propeller, is not implicated in this function. Here, we present the structure of the RbBP5 beta-propeller domain revealing a distinct, feature rich surface, dominated by clusters of Arginine residues. Our nuclear magnetic resonance binding data supports the hypothesis that in addition to the role of RbBP5 in catalytic activation, its beta-propeller domain is a platform for the recruitment of the MLL complexes to chromatin targets through its direct interaction with nucleic acids. The structure of the RbBP5 beta-propeller domain reveals a surface with potential nucleic acid binding sites.,Mittal A, Hobor F, Zhang Y, Martin SR, Gamblin SJ, Ramos A, Wilson JR Nucleic Acids Res. 2018 Apr 20;46(7):3802-3812. doi: 10.1093/nar/gky199. PMID:29897600[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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