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

Abstract:

: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.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Takeuchi F,Hashimoto E,Yamamura H

doi

10.1093/oxfordjournals.jbchem.a123837

keywords:

subject

Has Abstract

pub_date

1992-06-01 00:00:00

pages

788-92

issue

6

eissn

0021-924X

issn

1756-2651

journal_volume

111

pub_type

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