May 13, 1976

Multiple forms of histone acetyltransferases in the cytosol of calf endometrium

Biochimica Et Biophysica Acta
S R Harvey, P R Libby

Abstract

The histone acetyltransferase (EC 2.3.1.-) activity of calf endometrium cytosol has been separated into three separate activities by stepwise chromatography on DEAE-cellulose. In addition to differential elution from the DEAE-cellulose, the three activities are differentiated by their pH optima, preferences for histone subfractions as substrates, and stability to heat denaturation. Peak I has an optimum of pH 8.7 and preferentially acetylates histones F2b and F3; Peak II has an optimum of pH 8.5, and preferentially acetylates histone F2al followed by histone F2b; Peak III has an optimum of pH 9.5, and had similar specificity to Peak II. Peak III is appreciably more stable at 60 degrees C than is Peak II. None of the peaks transferred acetate to other proteins tested or to tRNA. These studies suggest the presence of multiple histone acetyltransferases in tissue cytosols.

  • References1
  • Citations3

References

Mentioned in this Paper

Endometrium
Chromatography, DEAE-Cellulose
Hot Temperature
Bos indicus
Histone H7
HAT1
Acetyltransferase
Hydrogen-Ion Concentration
Cytoplasmic Matrix
Metazoa

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