Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader.
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ABSTRACT:
SUBMITTER: Lee YJ
PROVIDER: S-EPMC5072174 | biostudies-literature | 2016 Oct
REPOSITORIES: biostudies-literature
Publications
Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader.
Lee Yan-Jiun YJ Schmidt M J MJ Tharp Jeffery M JM Weber Annemarie A Koenig Amber L AL Zheng Hong H Gao Jianmin J Waters Marcey L ML Summerer Daniel D Liu Wenshe R WR
Chemical communications (Cambridge, England) 20161001 85
Fluorophenylalanines bearing 2-5 fluorine atoms at the phenyl ring have been genetically encoded by amber codon. Replacement of F59, a phenylalanine residue that is directly involved in interactions with trimethylated K9 of histone H3, in the Mpp8 chromodomain recombinantly with fluorophenylalanines significantly impairs the binding to a K9-trimethylated H3 peptide. ...[more]
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