Structural Basis of Histone H4 Recognition by p55

Journal Article · Tue Jan 01 00:00:00 EST 2008 · Genes and Development

DOI:https://doi.org/10.1101/gad.1653308· OSTI ID:959673

Song, J; Garlick, J; Kingston, R

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 ?-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.

• Research Organization: Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: DE-AC02-98CH10886
• OSTI ID: 959673
• Report Number(s): BNL-82659-2009-JA; GEDEEP; TRN: US201016%%817
• Journal Information: Genes and Development, Vol. 22; ISSN 0890-9369
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
CRYSTAL STRUCTURE
DROSOPHILA
HISTONES
MODIFICATIONS
PROTEINS
national synchrotron light source