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

Affiliation

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.

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