Multiple forms of histone acetyltransferases in the cytosol of calf endometrium.
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.
D000085:Acetates / Q000378:metabolism; D000123:Acetyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D002848:Chromatography, DEAE-Cellulose; D003600:Cytosol / Q000201:enzymology*; D004717:Endometrium / Q000201:enzymology*; D005260:Female; D006657:Histones / Q000378:metabolism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration
D000085:Acetates; D006657:Histones; D000123:Acetyltransferases