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The phosphorylated site of calf thymus F2b histone by the cyclic AMP-dependent protein kinase

Naturevolume 254page88 (1975) | Download Citation

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Abstract

THE phosphorylation of histones is a complex process which occurs at different stages of the cell cycle1–3. Different types of histone kinases are responsible for the phosphorylation of the seryl (or threonyl) residues of the histone fractions. One of them is the ubiquitous cyclic AMP-dependent protein kinase4,5, whereas the histone kinase predominant in mitotic cells is not activated by the cyclic nucleotide6. The cyclic AMP-dependent enzyme of rat liver, phosphorylates the seryl residue in the position 37 of calf thymus F1 histone, and the growth associated histone kinase catalyses the phosphorylation of other seryl and threonyl residues of the F1 fraction4–6.

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Author information

Affiliations

  1. Institute of Biochemistry, Semmelweis University Medical School

    • ANNA FARAGO
    • , TIBOR ROMHANYI
    • , FERENC ANTONI
    •  & ATTILA TAKATS
  2. Department of Biochemistry, Lóránd Eötvös University, Budapest, 1088, Hungary

    • FERENC FABIAN

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https://doi.org/10.1038/254088a0

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