Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain

  • Nat Struct Mol Biol. 2010 Aug;17(8):1027-9. doi: 10.1038/nsmb.1856.
Daesung Kim  1 ,  Bartlomiej J Blus ,  Vikas Chandra ,  Pengxiang Huang ,  Fraydoon Rastinejad ,  Sepideh Khorasanizadeh
Affiliations
  • 1. Department of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, Virginia, USA.
PMID: 20657587 DOI: 10.1038/nsmb.1856
Abstract

MSL3 resides in the MSL (male-specific lethal) complex, which upregulates transcription by spreading the histone H4 Lys16 (H4K16) acetyl MARK. We discovered a DNA-dependent interaction of MSL3 chromodomain with the H4K20 monomethyl MARK. The structure of a ternary complex shows that the DNA minor groove accommodates the histone H4 tail, and monomethyllysine inserts in a four-residue aromatic cage in MSL3. H4K16 acetylation antagonizes MSL3 binding, suggesting that MSL function is regulated by a combination of post-translational modifications.