Recognition of stapled histone H3K4me3 peptides by epigenetic reader proteins

Chem Commun (Camb). 2022 Nov 1;58(87):12196-12199. doi: 10.1039/d2cc04294k.

Abstract

The flexible N-terminal histone tails are a subject of numerous posttranslational modifications, including methylation. We report development of stapled histone peptides bearing trimethyllysine as ligands for epigenetic reader proteins. Stronger or weaker binding affinities have been observed for stapled histone peptides relative to linear histones, indicating that selectivity towards reader proteins can be achieved.

MeSH terms

  • Epigenesis, Genetic
  • Histones* / metabolism
  • Methylation
  • Peptides* / metabolism

Substances

  • histone H3 trimethyl Lys4
  • Histones
  • Peptides