Article
Histone octamer function in vivo: mutations in the dimer-tetramer interfaces disrupt both gene activation and repression.
The EMBO journal - 1 May 1997
Santisteban M S, Arents G, Moudrianakis E N, Smith M M
Abstract excerpt
Within the core histone octamer each histone H4 interacts with each H2A-H2B dimer subunit through two binding surfaces. Tyrosines play a central role in these interactions with H4 tyrosines 72 and 88 contacting one H2A-H2B dimer subunit, and tyrosine 98 contacting the other. To investigate the roles of these interactions in vivo, we made site-directed amino acid substitutions at each of these tyrosine residues....
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