4.7 Article

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

Journal

CHEMICAL COMMUNICATIONS
Volume 52, Issue 85, Pages 12606-12609

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c6cc05959g

Keywords

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Funding

  1. National Institute of Health [CA161158, GM102735]
  2. National Science Foundation [CHE-1148684, CHE-1112188, CHE-1306977, DGE-1144081]
  3. Welch Foundation [A-1715]
  4. Deutsche Forschungsgemeinschaft [SU 726/6-1 in SPP1623]
  5. Division Of Chemistry
  6. Direct For Mathematical & Physical Scien [1148684] Funding Source: National Science Foundation

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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.

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