Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis

Beat Fierz, Sinan Kilic, Aaron R. Hieb, Karolin Luger, Tom W. Muir

Research output: Contribution to journalArticlepeer-review

78 Scopus citations


Post-translational modifications (PTMs) of histones are an essential feature in the dynamic regulation of chromatin. One of these modifications, ubiquitylation, has been speculated to directly influence the stability of the nucleosome, which represents the basic building block of chromatin. Here we report a strategy for the semisynthesis of site-specifically ubiquitylated histone H2A (uH2A). This branched protein was generated through a three-piece expressed protein ligation approach including a traceless ligation at valine. uH2A could be efficiently incorporated into nucleosomes, thereby opening the way to detailed biochemical and biophysical studies on the function of this PTM. Accordingly, we used uH2A, as well as a previously generated ubiquitylated H2B, in chaperone-coupled nucleosome stability assays to demonstrate that the direct effect of ubiquitylated histones on nucleosomal stability is in fact modest.

Original languageEnglish (US)
Pages (from-to)19548-19551
Number of pages4
JournalJournal of the American Chemical Society
Issue number48
StatePublished - Dec 5 2012

All Science Journal Classification (ASJC) codes

  • General Chemistry
  • Biochemistry
  • Catalysis
  • Colloid and Surface Chemistry


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