Abstract
MSL3 resides in the MSL (male-specific-lethal) complex that upregulates transcription by spreading the H4K16 acetyl-mark. We discovered a DNA-dependent interaction of MSL3 chromodomain with the histone H4K20 monomethyl-mark. Structure of a ternary complex shows DNA minor groove accommodates the histone H4 tail, and monomethyllysine inserts in a four-residue aromatic cage in MSL3. Histone H4K16 acetyl-mark antagonizes MSL3 binding, suggesting MSL function is regulated by a combination of post-translational modifications.
Full Text 
Sign-in/Register to access full text options
Sign-in/Register to access full text options 
Published version (
Free)
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
