Phosphorylation of histone H2A by protein kinase C and identification of the phosphorylation site.

Phosphorylation of histone H2A by protein kinase C and identification of the phosphorylation site. Research Abstract Details 

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Phosphorylation of histone H2A by protein kinase C and identification of the phosphorylation site. Abstract Text:

F Takeuchi,E Hashimoto,H Yamamura,

In regenerating rat liver, nuclear protein histone H2A was shown to be phosphorylated on its amino-terminal serine residue [Sung et al. (1971) J. Biol. Chem. 246, 1358-1364], but the protein kinase which phosphorylates this residue has not been identified. To evaluate the possibility that protein kinase C can phosphorylate this residue, calf thymus histone H2A was 32P-labeled by incubation with [gamma-32P]ATP and highly purified protein kinase C from rat brain in the presence of calcium and phospholipid. About 1 mol of 32P was incorporated per mol of histone H2A and the Km and apparent Vmax of the reaction were calculated to be 2.1 microM and 0.35 mumol/min/mg, respectively. So histone H2A seemed to be a good substrate for protein kinase C. Further, the proteolytic phosphopeptides of 32P-labeled histone H2A were isolated by means of a series of column chromatographies and analyzed for their amino acid compositions. Comparison of the data with the known primary structure of histone H2A revealed their amino acid sequence as 1Ser-Gly-Arg. These data suggest that protein kinase C may be a candidate for the protein kinase which phosphorylates the amino-terminal serine residue of histone H2A during the regeneration of rat liver.

Phosphorylation of histone H2A by protein kinase C and identification of the phosphorylation site. Publishing Authors By Initials

F Takeuchi,E Hashimoto,H Yamamura,

For similar animals: animal population groups: animals, inbred strains: rats, inbred strains research abstracts see: animals: animal population groups: animals, inbred strains: rats, inbred strains research

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Phosphorylation of histone H2A by protein kinase C and identification of the phosphorylation site. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 111

Page Numbers: 788-92

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jun

YEAR: 1992

Phosphorylation of histone H2A by protein kinase C and identification of the phosphorylation site. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Phosphorylation of histone H2A by protein kinase C and identification of the phosphorylation site. Keywords Mesh Terms:

KEYWORDS: Rats, Inbred Strains

MESH TERMS: metabolism

Chemical & Substance for Abstract: Phosphorylation of histone H2A by protein kinase C and identification of the phosphorylation site. Information

Substance Name: Protein Kinase C

Registry Number: EC 2.7.11.13

Grant and Affiliation Information for Phosphorylation of histone H2A by protein kinase C and identification of the phosphorylation site.

AFFILIATION: Department of Biochemistry, Fukui Medical School.

Country: JAPAN

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MEDLINETA: J Biochem

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