A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity?

Trends Biochem Sci. 2002 Mar;27(3):115-7. doi: 10.1016/s0968-0004(02)02058-3.

Abstract

A new subfamily of two-domain histone acetyltransferases (HATs) related to Elp3 has been identified. In addition to a HAT domain in the C terminus, these proteins have an N-terminal domain similar to the catalytic domain of S-adenosylmethionine radical enzymes. Two-domain organization is preserved in evolution, suggesting that both enzymatic activities are functionally or mechanistically coupled and directed towards highly conserved substrates. The functional implications of this similarity and a possible role for Elp3-related proteins as histone demethylases are discussed.

Publication types

  • Review

MeSH terms

  • Acetyltransferases / chemistry*
  • Acetyltransferases / genetics
  • Acetyltransferases / metabolism*
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Catalysis
  • Catalytic Domain / physiology*
  • Histone Acetyltransferases
  • Histones / chemistry
  • Histones / metabolism
  • Humans
  • Methylation
  • Molecular Sequence Data
  • Multigene Family
  • Saccharomyces cerevisiae Proteins*
  • Sequence Homology, Amino Acid

Substances

  • Histones
  • Saccharomyces cerevisiae Proteins
  • Acetyltransferases
  • Histone Acetyltransferases