Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain.
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.
Kim
Daesung
D
Department of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, Virginia, USA.
Blus
Bartlomiej J
BJ
Chandra
Vikas
V
Huang
Pengxiang
P
Rastinejad
Fraydoon
F
Khorasanizadeh
Sepideh
S
D000818:Animals; D004247:DNA / Q000378:metabolism*; D029721:Drosophila Proteins / Q000737:chemistry* / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000378:metabolism*; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism; D008745:Methylation; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
D029721:Drosophila Proteins; D006657:Histones; D010455:Peptides; D021122:Protein Subunits; D004247:DNA; D008239:Lysine