[来自大鼠肝核基质的对H1组蛋白具有特异性的DNA和三磷酸核苷酸激活蛋白酶]

[DNA and nucleotide triphosphate-activated proteinase from rat liver nuclear matrix specific for H1 histone].

作者信息

Kutsyĭ M P, Gaziev A I

出版信息

Mol Biol (Mosk). 1988 Sep-Oct;22(5):1430-6.

Abstract

The action of DNA and nucleotide phosphate on histone hydrolysis by nuclear matrix preparations from rat liver has been studied. It is shown that proteinase specific for H1 histone is associated with the nuclear matrix. This proteinase is activated by denatured DNA and by DNA treatment with DNase I or gamma-irradiation, but it is not activated by UV-irradiated DNA. In the presence of nucleotide triphosphates, particularly GTP and ATP, proteolysis of H1 histone is markedly increased. The nuclear matrix proteinase specific for H1 histone and activated by DNA or GTP and ATP appears inhibited by antipain, leupeptin, phenylmethylsulfonyl fluoride (the inhibitors of serine proteinases) as well as by dithiotreitol.

摘要

研究了大鼠肝脏核基质制剂中DNA和核苷酸磷酸盐对组蛋白水解的作用。结果表明，对H1组蛋白具有特异性的蛋白酶与核基质相关。这种蛋白酶可被变性DNA以及经DNA酶I处理或γ射线照射的DNA激活，但不能被紫外线照射的DNA激活。在存在三磷酸核苷酸，特别是GTP和ATP的情况下，H1组蛋白的蛋白水解作用明显增强。对H1组蛋白具有特异性且被DNA或GTP和ATP激活的核基质蛋白酶，似乎受到抗蛋白酶、亮抑酶肽、苯甲基磺酰氟（丝氨酸蛋白酶抑制剂）以及二硫苏糖醇的抑制。