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Published online before print April 28, 2008, 10.1101/gad.1653308
GENES & DEVELOPMENT 22:1313-1318, 2008
©2008 by Cold Spring Harbor Laboratory Press; ISSN 0890-9369/ $5.00
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RESEARCH COMMUNICATION

Structural basis of histone H4 recognition by p55

Ji-Joon Song, Joseph D. Garlick, and Robert E. Kingston1

Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts 02114, USA; Department of Genetics, Harvard Medical School, Boston, Massachusetts 02114, USA

p55 is a common component of many chromatin-modifying complexes and has been shown to bind to histones. Here, we present a crystal structure of Drosophila p55 bound to a histone H4 peptide. p55, a predicted WD40 repeat protein, recognizes the first helix of histone H4 via a binding pocket located on the side of a β-propeller structure. The pocket cannot accommodate the histone fold of H4, which must be altered to allow p55 binding. Reconstitution experiments show that the binding pocket is important to the function of p55-containing complexes. These data demonstrate that WD40 repeat proteins use various surfaces to direct the modification of histones.

[Keywords: p55; Nurf55; RbAp48; histone; chromatin; WD40]

Received January 18, 2008; revised version accepted March 13, 2008.

1 Corresponding author.

E-MAIL kingston{at}molbio.mgh.harvard.edu; FAX (617) 643-2119.

Supplemental material is available at http://www.genesdev.org.

Article published online ahead of print. Article and publication date are online at http://www.genesdev.org/cgi/doi/10.1101/gad.1653308.


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