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

Kutsyĭ, M.P.; Gaziev, A.I.

Molekuliarnaia Biologiia 22(5): 1430-1436

1988

ISSN/ISBN: 0026-8984
PMID: 3065619
Document Number: 323929
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.

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