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• W2765943668 abstract "Biochem. J. (1970) 119, 665-672 Printed in Great Britain Histone-Acetylating Enzyme of Brain BY S. C. BONDY, SIDNEY ROBERTS AND BEATRICE S. MORELOS Department of Biological Chemistry, School of Medicine and the Brain Research Institute, University of California Center for the Health Sciences, Los Angeles, Calif. 90024, U.S.A. (Received 1June1970) 1. Acetylation of histones by an enzyme system derived from rat brain and liver (histone acetylase) was studied by using [l- 14 C]acetyl-CoA as the acetyl group donor. 2. The activity of this enzyme was largely confined to the nucleus. 3. Histone-acetylating activity of cerebral nuclei purified by centrifugation through l.9M-sucrose was not altered by the presence of the cytoplasmic fraction. 4. Cere- bral nuclei from adult rats exhibited greater histone-acetylating activity than did the corresponding preparation from newborn animals. 5. Nuclear acetylating activity was higher in brain than in liver of adult rats but not in newborn animals. 6. The partially purified enzyme from cerebral nuclei, prepared by ammonium sulphate fractionation of an acetone-dried powder, specifically catalysed histone acetylation. 7. Poly lysine, protamine, serum albumin and y-globulin were not enzymically acetylated by this preparation. 8. Soluble acetylating preparations from both brain and liver nuclei were more active towards arginine-rich F3 and slightly lysine-rich F2a and F2b histone fractions than towards the lysine-rich Fl fraction. 9. Enzymic acetylation of chromatin-bound proteins was much less extensive than that of free histones. I 0. The high histone acetylase activity in mature brain may reflect the importance of this process in the genetic control of cerebral function. The synthesis of RNA and p;rotein in the mature brain appears to proceed at rates comparable with those observed in other active tissues of the adult animal (Zomzely, Roberts & Rapaport, 1964; Bondy, 1966; Jacob, Stevenin, Jund, Judes & Mandel, 1966; Roberts & Zomzely, 1966). Evidence has been presented that these processes are un- usually sensitive to changes in the environment (Roberts, Zomzely & Bondy, 1970). Since the adult brain possesses a relatively stable DNA population (Adrian & Walker, 1962; Adams, 1966), alterations in genetic expression in this organ must be dependent on mechanisms that proceed at a rapid rate and are highly responsive to regulatory influences. Histones and other nuclear proteins are thought to repress the genome by interacting with chromoso- mal DNA (Bonner et al. 1968). Gene expression may involve, in part, modification of these histones and resultant weakening of their association with DNA. The presence of acetylated lysine groups has been demonstrated in histones derived from various plant and animal sources (Allfrey, 1968; DeLange, Fambrough, Smith & Bonner, 1969). The degree of histone acetylation may be related to the physiological state of the tissue (Pogo, Pogo, Allfrey & Mirsky, 1968). For example, selective acetylation of certain bound histones, by decreasing their basicity, may favour their dissociation from DNA (Gershey, Vidali & Allfrey, 1968; Libby, 1968). The present investigations were initiated in an attempt to assess the significance of histone acetylation in the regulation of RNA and protein synthesis in the brain. This paper describes the preparation and some characteristics of a cerebral enzyme system (histone-acetyl-CoA acetyltrans- ferase) that is confined to the nuclear fraction of rat brain and acetylates histones selectively. This enzyme is highly active in the mature brain and may reflect the dynamic state of the cerebral genome in this organ. EXPERIMENTAL Preparation of c11toplasm and purified nuclei. Rats of an inbred Sprague-Dawley strain were used. Newborn animals were 1-16 h old. Adult animals were maintained after weaning on Purina laboratory chow ad libitum until they were 6 weeks old. Newborn rats were killed by decapitation; adult animals were killed by exsanguination from the abdominal aorta under light anaesthesia with sodium pentobarbital (Nembutal). Bra.ins and livers were rapidly removed and placed in cold 0.32M-sucrose. All subsequent procedures were carried out at 0-4°0. TissueA were homogenized by hand in 12 vol. of cold 0.32 M-sucroRe" @default.
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• W2765943668 date "1970-01-01" @default.
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• W2765943668 title "Histone acetylating enzyme of the brain" @default.
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