ACETYLATION OF HISTONES BY A KINASE FROM RAT LIVER NUCLEI

A variety of proteins have been reported to contain N-acetyl groups (Harris, 1959, Harris and Hindley, 1961, Margoliash et al., 1961, Marshall and Neuberger, 1961, Narita, 1958, Phillips, 1963, Satake et al., 1963, Schroeder et al., 1962, Titani et al., 1962). The reactions which form terminal acetyl groups in proteins and their biological significance are not understood. The detction of acetyl groups in calf thymus histones (Phillips, 1963) and the finding that chemically acetylated histones are less effective inhibitors of the DNA-dependent RNA polymerase in vitro led to the hypothesis that acetylation of histones could be important in the regulation of RNA synthesis (Allfrey et al., 1964, Pogo et al., 1966). Isolated calf thymus (Allfrey et al., 1964) and rat liver nuclei (Gallwitz and Sekeris, in prep.) acetylate histones in vitro and enzymes which incorporate C14-acetate into histones have been demonstrated in pigeon liver (Nohara et al., 1966). This paper reports the transfer of acetate from coenzyme A to rat liver histones by an acetokinase from pure rat liver nuclei. © 1968.