Ontology highlight
ABSTRACT:
SUBMITTER: Pieters BJ
PROVIDER: S-EPMC4589357 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
Pieters Bas J G E BJ Meulenbroeks Erik E Belle Roman R Mecinović Jasmin J
PloS one 20150930 9
Several reader domain proteins that specifically recognize methyllysine-containing histones contain the negatively-charged aspartate or glutamate residues as part of the aromatic cage. Herein, we report thermodynamic analyses for the recognition of histone H3K4me3 and H3K4me2 by the tandem tudor domain of Sgf29 and its recognition site variants. Small uncharged and large aromatic substitutions on the Asp266 site resulted in a significant decrease in binding affinities for both H3K4me3 and H3K4me ...[more]