Thiirane linkers directed histone H2A diubiquitination suggests plasticity in 53BP1 recognition

Chem Commun (Camb). 2019 Oct 17;55(84):12639-12642. doi: 10.1039/c9cc05526f.

Abstract

Polyubiquitination with diverse linkages on histones provides another layer of accuracy and complexity for epigenetic regulation, which is rarely studied. Herein, K27 or K48-diubiquitin modified H2A analogues were chemically synthesized using thiirane linkers. These permitted in vitro binding studies suggested the plasticity of ubiquitin chains in 53BP1 recognition.

MeSH terms

  • Histones / chemistry*
  • Polyubiquitin / chemistry*
  • Protein Binding
  • Recombinant Proteins / chemistry
  • Sulfides / chemistry*
  • Tumor Suppressor p53-Binding Protein 1 / chemistry*
  • Ubiquitination

Substances

  • Histones
  • Recombinant Proteins
  • Sulfides
  • Tumor Suppressor p53-Binding Protein 1
  • Polyubiquitin
  • ethylene sulfide