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Submitted on May 24, 2002
Pharmaceutical Chemistry, University of California, San Francisco, CA 94143
Corresponding Author: alb{at}itsa.ucsf.edu
The acetylation isoforms of histone H4 from butyrate treated HeLa cells were separated by C4 reversed phase HPLC and by polyacrylamide gel electrophoresis. Histone H4 bands were excised and digested in-gel with the endoprotease trypsin. MALDI-TOF mass spectrometry was used to characterize the level of acetylation and Nano-ESI/MS/MS analysis of the acetylated peptides was used to determine the exact sites of acetylation. Although there are 15 acetylation sites possible, only four acetylated peptide sequences were actually observed. The tetra-acetylated form is modified at lysines 5, 8, 12 and 16, the tri-acetylated form at lysines 8, 12 and 16, and the di-acetylated form at lysines 12 and 16. The only significant amount of mono-acetylated form was found at position 16. These results are consistent with the hypothesis of a "zip" model whereby acetylation of histone H4 proceeds in the direction of from Lys16 to Lys5 and deacetylation proceeds in the reverse direction. Histone acetylation and deacetylation are coordinated processes leading to a nonrandom distribution of isoforms. Our results also revealed that lysine 20 is dimethylated in all modified isoforms as well as the non-acetylated isoform of H4.
Revised on July 9, 2002
Accepted on July 16, 2002
Histone acetylation and deacetylation: identification of acetylation and methylation sites of HeLa histone H4 by mass spectrometry
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