The Saccharomyces cerevisiae histone H2A variant Htz1 is acetylated by NuA4

Genes Dev. 2006 Mar 15;20(6):660-5. doi: 10.1101/gad.1388106.


The histone H2A variant H2A.Z (Saccharomyces cerevisiae Htz1) plays roles in transcription, DNA repair, chromosome stability, and limiting telomeric silencing. The Swr1-Complex (SWR-C) inserts Htz1 into chromatin and shares several subunits with the NuA4 histone acetyltransferase. Furthermore, mutants of these two complexes share several phenotypes, suggesting they may work together. Here we show that NuA4 acetylates Htz1 Lys 14 (K14) after the histone is assembled into chromatin by the SWR-C. K14 mutants exhibit specific defects in chromosome transmission without affecting transcription, telomeric silencing, or DNA repair. Function-specific modifications may help explain how the same component of chromatin can function in diverse pathways.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Acetylation
  • Acetyltransferases / metabolism*
  • Amino Acid Sequence
  • Chromosomes, Fungal
  • Histone Acetyltransferases
  • Histones / chemistry
  • Histones / metabolism*
  • Molecular Sequence Data
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Sequence Homology, Amino Acid


  • Histones
  • Htz1 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Acetyltransferases
  • Histone Acetyltransferases
  • NuA4 protein, S cerevisiae