Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader

Yan-Jiun Lee; M. J. Schmidt; Jeffery M. Tharp; Annemarie Weber; Amber L. Koenig; Hong Zheng; Jianmin Gao; Marcey L. Waters; Daniel Summerer; Wenshe R. Liu

doi:10.1039/C6CC05959G

Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader†

Yan-Jiun Lee,^a M. J. Schmidt,^b Jeffery M. Tharp,^a Annemarie Weber,^b Amber L. Koenig,^c Hong Zheng,^d Jianmin Gao,^d Marcey L. Waters,^c Daniel Summerer*^e and Wenshe R. Liu*^a

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* Corresponding authors

^a Department of Chemistry, Texas A&M University, College Station, TX 7743, USA
E-mail: wliu@chem.tamu.edu

^b Department of Chemistry, University of Konstanz, 78457 Konstanz, Germany

^c Department of Chemistry, Boston College, Boston, MA 02467, USA

^d Department of Chemistry, University of North Carolina, Chapel Hill, NC 27599, USA

^e Department of Chemistry and Chemical Biology, Technical University of Dortmund, 44227 Dortmund, Germany
E-mail: Daniel.summerer@tu-dortmund.edu

Abstract

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.

Chemical Communications

Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader†

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Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader

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