Structural highlights
Function
[MSL3_DROME] The MSL proteins are essential for elevating transcription of the single X chromosome in the male (X chromosome dosage compensation). Mle, msl-1 and msl-3 are colocalized on the X chromosome. Each of the MSL proteins requires all the other MSLs for wild-type X-chromosome binding.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain.,Kim D, Blus BJ, Chandra V, Huang P, Rastinejad F, Khorasanizadeh S Nat Struct Mol Biol. 2010 Aug;17(8):1027-9. Epub 2010 Jul 25. PMID:20657587[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gorman M, Franke A, Baker BS. Molecular characterization of the male-specific lethal-3 gene and investigations of the regulation of dosage compensation in Drosophila. Development. 1995 Feb;121(2):463-75. PMID:7768187
- ↑ Kim D, Blus BJ, Chandra V, Huang P, Rastinejad F, Khorasanizadeh S. Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain. Nat Struct Mol Biol. 2010 Aug;17(8):1027-9. Epub 2010 Jul 25. PMID:20657587 doi:10.1038/nsmb.1856
