The site of histone H2b phosphorylated by a cyclic nucleotide independent histone kinase

T. Romhányi, J. Seprödi, F. Antoni, K. Nikolics, G. Mészáros, A. Faragó

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

A cyelic nucleotide independent histone kinase was demonstrated in bovine thymus extract. This enzyme was very similar to that found previously in the cytoplasm and nucleus of human tonsillar lymphocytes (Faragó et al., 1973, Biochim. Biophys. Acta 297, 517 and 1974, ibid 370, 459). High-performance liquid chromatography of the tryptic phosphopeptides of calf thymus histones H1 and H2b phosphorylated by the histone kinase or by the catalytic subunit of cylic AMP dependent protein kinase showed that the intrinsic substrate specificity of these enzymes differed significantly. Under our experimental conditions the histone kinase phosphorylated preferentially the Ser-32 residue, and it did not phosphorylate the Ser-36 residue of histone H2b, while Ser-36 was phosphorylated preferentially by the cyclic AMP dependent protein kinase. A peptide containing the amino acid sequence of histone H2b from Gly-26 to Lys-34 (Gly-Lys-Lys-Arg-Lys-Arg-Ser-Arg-Lys-Ala) was synthesized. This peptide was a competitive inhibitor of histone H1 phosphorylation by the histone kinase and it was also a substrate for this enzyme.

Original languageEnglish
Pages (from-to)57-62
Number of pages6
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume701
Issue number1
DOIs
Publication statusPublished - Feb 4 1982

Keywords

  • Cyclic nucleotide dependence
  • Histone H2b
  • Histone kinase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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