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    FEBS Lett. 1988 Jul 4;234(1):31-4.

    Identification of the phosphoserine residue in histone H1 phosphorylated by protein kinase C.

    Jakes S, Hastings TG, Reimann EM, Schlender KK.

    Department of Pharmacology, Medical College of Ohio, Toledo 43699.

    The site-specific phosphorylation of bovine histone H1 by protein kinase C was investigated in order to further elucidate the substrate specificity of protein kinase C. Protein kinase C was found to phosphorylate histone H1 to 1 mol per mol. Using N-bromosuccinimide and thrombin digestions, the phosphorylation site was localized to the globular region of the protein, containing residues 71-122. A tryptic peptide containing the phosphorylation site was purified. Modification of the phosphoserine followed by amino acid sequence analysis demonstrated that protein kinase C phosphorylated histone H1 on serine 103. This sequence, Gly97-Thr-Gly-Ala-Ser-Gly-Ser(PO4)-Phe-Lys105, supports the contention that basic amino acid residues C-terminal to the phosphorylation site are sufficient determinants for phosphorylation by protein kinase C.

    PMID: 3134256 [PubMed - indexed for MEDLINE]

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