Two species of histone acetyltransferase in rat liver nuclei.
Subcellular localization of histone acetyltransferase was studied in rat liver cells. Two histone acetyltransferases, designated NI and NII, were identified in the nuclear fraction, and an additional two acetyltransferases, termed CI and CII, were separated from the cytoplasmic fraction. These acetyltransferases exhibited different substrate specificities toward free and nucleosomal histones. The enzymes NI and NII represented major histone acetyltransferase activities in rat liver nuclei, and they were further differentiated by DNA-binding properties, subnuclear localization, and reaction kinetics. While the NI enzyme exhibited an intersecting initial velocity kinetic, the NII enzyme followed a ping-pong initial velocity pattern. These results show the multiple occurrence of histone acetyltransferases in nuclear and cytoplasmic fractions, events which may reflect the complexities of histone acetylation.
D000123:Acetyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology*; D002846:Chromatography, Affinity; D004247:DNA; D051548:Histone Acetyltransferases; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008836:Micrococcal Nuclease; D051381:Rats; D029701:Saccharomyces cerevisiae Proteins
D007527:Isoenzymes; D029701:Saccharomyces cerevisiae Proteins; D004247:DNA; D000123:Acetyltransferases; D051548:Histone Acetyltransferases; D008836:Micrococcal Nuclease