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

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.

SUBMITTER: Kim D

PROVIDER: S-EPMC2924628 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

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

Kim Daesung D Blus Bartlomiej J BJ Chandra Vikas V Huang Pengxiang P Rastinejad Fraydoon F Khorasanizadeh Sepideh S

Nature structural & molecular biology 20100725 8

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 ...[more]

PMID: 20657587

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