Transcription-linked Acetylation by Gcn5p of Histones H3 and H4 at Specific Lysines

Nature. 1996 Sep 19;383(6597):269-72. doi: 10.1038/383269a0.

Abstract

The yeast transcriptional adaptor, Gcn5p, is a catalytic subunit of a nuclear (type A) histone acetyltransferase linking histone acetylation to gene activation. Here we report that Gcn5p acetylates histones H3 and H4 non-randomly at specific lysines in the amino-terminal domains. Lysine 14 of H3 and lysines 8 and 16 of H4 are highly preferred acetylation sites for Gcn5p. We also demonstrate that lysine 9 is the preferred position of acetylation in newly synthesized yeast H3 in vivo. This finding, along with the fact that lysines 5 and 12 in H4 are predominant acetylation sites during chromatin assembly of many organisms, indicates that Gcn5p acetylates a distinct set of lysines that do not overlap with those sites characteristically used by type B histone acetyltransferases for histone deposition and chromatin assembly.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylation
  • Acetyltransferases / metabolism*
  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chickens
  • DNA-Binding Proteins*
  • Fungal Proteins / metabolism*
  • Histone Acetyltransferases
  • Histones / metabolism*
  • Lysine / metabolism*
  • Molecular Sequence Data
  • Protein Kinases / metabolism*
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae Proteins*
  • Substrate Specificity
  • Tetrahymena thermophila / metabolism
  • Transcription, Genetic*

Substances

  • DNA-Binding Proteins
  • Fungal Proteins
  • Histones
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • Acetyltransferases
  • Histone Acetyltransferases
  • Protein Kinases
  • Lysine