Histone acetylation facilitates association of nucleosomes with SET domain of ALL-1 methyltransferase in vitro

Biochem Biophys Res Commun. 2010 Jun 18;397(1):112-6. doi: 10.1016/j.bbrc.2010.05.080. Epub 2010 May 20.

Abstract

The inheritable methylation pattern of gene activity, created upon cell differentiation, is further maintained by the "SET" (methyltransferase)-domain proteins. However, it is still not clear how SET-proteins can decide on the required gene activity state and the way their chromatin association is maintained. Here we have found that high levels of histone acetylation--the hallmarks of active chromosome regions in vivo--can increase the affinity of reconstituted nucleosomes to the SET domain of ALL-1 histone methyltransferase in a defined system in vitro.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • HeLa Cells
  • Histone-Lysine N-Methyltransferase / metabolism*
  • Histones / metabolism*
  • Humans
  • Myeloid-Lymphoid Leukemia Protein / metabolism*
  • Nucleosomes / enzymology*
  • Protein Structure, Tertiary

Substances

  • Histones
  • KMT2A protein, human
  • Nucleosomes
  • Myeloid-Lymphoid Leukemia Protein
  • Histone-Lysine N-Methyltransferase