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Identification of the phosphoserine residue in histone H1 phosphorylated by protein kinase C
Author(s) -
Jakes Scott,
Hastings Teresa G.,
Reimann Erwin M.,
Schlender Keith K.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81296-1
Subject(s) - phosphoserine , biochemistry , phosphorylation , map2k7 , protein phosphorylation , protein kinase a , cyclin dependent kinase 2 , c raf , mitogen activated protein kinase kinase , histone h1 , serine , microbiology and biotechnology , biology , chemistry , histone , gene
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, Gly 97 ‐Thr‐Gly‐Ala‐Ser‐Gly‐Ser(PO 4 )‐Phe‐Lys 105 , supports the contention that basic amino acid residues C‐terminal to the phosphorylation site are sufficient determinants for phosphorylation by protein kinase C.