Work

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

Year: 2016

Type: article

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.

Source: Chemical Communications

DOI: 10.1039/c6cc05959g

Authors: 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

Institutions: Texas A&M University, University of Konstanz, Boston College, University of North Carolina at Chapel Hill, TU Dortmund University

Language: English

Topic: Epigenetics and DNA Methylation

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Funders: National Science Foundation, Welch Foundation, Deutsche Forschungsgemeinschaft, National Cancer Institute, National Institute of General Medical Sciences, Division of Chemistry

Awards: CAREER: Site-specific dual-labeling of a protein through two genetically incorporated noncanonical amino acids, G1815005394, Targeted Modification of Membrane Lipids, Phage Display with Two Genetically Incorporated Noncanonical Amino Acids, G3863427225, G4611873998, G4992489664, G6131505737, G6553094674, G6810536968, G7455009664, Mechanistic Studies of Molecular Recognition of Methylated Lysine and Arginine, Develop Conditionaly Charged Residues for the Design of Peptide Channels, Graduate Reserach Fellowship Program (GRFP)

OpenAlex ID: W2524066498

FWCI: 0.602

Cites: 55

Cited by: 34

Related to: 10