In vitro analysis of histone acetyltransferase activity

Methods. 2004 May;33(1):45-52. doi: 10.1016/j.ymeth.2003.10.019.


Interest in histone acetylation has risen dramatically in recent years. In the following report, we present methods for the analysis of histone acetyltransferase activity in vitro. Protocols are described for radiolabeling histone proteins and N-terminal "tail" peptides, and for the analysis of acetylation by immunoblotting. Techniques for acetylating immobilized histone peptides are also described.

Publication types

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

MeSH terms

  • Acetylation
  • Acetyltransferases / metabolism*
  • Electrophoresis, Polyacrylamide Gel / methods
  • HeLa Cells
  • Histone Acetyltransferases
  • Histones / metabolism*
  • Humans
  • Peptide Fragments / metabolism*


  • Histones
  • Peptide Fragments
  • Acetyltransferases
  • Histone Acetyltransferases