脑组蛋白乙酰化酶
Histone-acetylating enzyme of brain.
作者信息
Bondy S C, Roberts S, Morelos B S
出版信息
Biochem J. 1970 Oct;119(4):665-72. doi: 10.1042/bj1190665.
Abstract
- Acetylation of histones by an enzyme system derived from rat brain and liver (histone acetylase) was studied by using [1-(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 1.9m-sucrose was not altered by the presence of the cytoplasmic fraction. 4. Cerebral 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. Polylysine, protamine, serum albumin and gamma-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 F1 fraction. 9. Enzymic acetylation of chromatin-bound proteins was much less extensive than that of free histones. 10. The high histone acetylase activity in mature brain may reflect the importance of this process in the genetic control of cerebral function.
摘要
以[1-(14)C]乙酰辅酶A作为乙酰基供体，研究了源自大鼠脑和肝脏的酶系统（组蛋白乙酰化酶）对组蛋白的乙酰化作用。
该酶的活性主要局限于细胞核。
通过在1.9M蔗糖中离心纯化的脑细胞核的组蛋白乙酰化活性不受细胞质部分存在的影响。
成年大鼠的脑细胞核比新生动物相应的制剂表现出更高的组蛋白乙酰化活性。
成年大鼠脑中的核乙酰化活性高于肝脏，但新生动物中并非如此。
通过对丙酮干粉进行硫酸铵分级分离制备的脑细胞核部分纯化酶特异性催化组蛋白乙酰化。
聚赖氨酸、鱼精蛋白、血清白蛋白和γ球蛋白不会被该制剂酶促乙酰化。
来自脑和肝细胞核的可溶性乙酰化制剂对富含精氨酸的F3以及略富含赖氨酸的F2a和F2b组蛋白组分的活性比对富含赖氨酸的F1组分的活性更高。
染色质结合蛋白的酶促乙酰化程度远低于游离组蛋白。
成熟脑中高的组蛋白乙酰化酶活性可能反映了该过程在脑功能基因控制中的重要性。
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