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  • Title: A specific phosphoprotein phosphatase acts on histone H1 phosphorylated by protein kinase C.
    Author: Sahyoun N, LeVine H, McConnell R, Bronson D, Cuatrecasas P.
    Journal: Proc Natl Acad Sci U S A; 1983 Nov; 80(22):6760-4. PubMed ID: 6316323.
    Abstract:
    A phosphohistone phosphatase from rat liver cytosol acts specifically on histone H1 that is phosphorylated with the Ca2+-phospholipid-dependent protein kinase (protein kinase C). The apparent Km for 32P-labeled H1 is 1 microM; other histones or cytosolic proteins phosphorylated with protein kinase C or with cyclic AMP-dependent protein kinase are poor substrates for the phosphatase. The enzyme has been partially purified by gel-permeation chromatography and by utilizing a high-performance liquid chromatography ion-exchange column. The physical properties of this enzyme include a Stokes radius of 5.0 nm, a sedimentation coefficient (s20,w) of 7.0 S, and a Mr of 150,000. The detection of protein kinase as well as the specific phosphohistone phosphatase in purified rat liver nuclei suggests a physiologic role for a histone H1 phosphorylation-dephosphorylation cycle mediated by protein kinase C and the corresponding phosphohistone phosphatase.
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