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Dephosphorylation of phosphorylase kinase by a histone H1‐stimulated phosphoprotein phosphatase
Author(s) -
Mellgren Ronald L.,
Wilson Susan E.,
Schlender Keith K.
Publication year - 1984
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(84)80145-3
Subject(s) - dephosphorylation , phosphorylase kinase , histone h1 , glycogen phosphorylase , histone , histone methyltransferase , phosphatase , phosphorylation , chemistry , biochemistry , dusp6 , histone h2a , microbiology and biotechnology , biology , protein phosphatase 2 , enzyme , gene
A histone H1‐stimulated protein phosphatase isolated from rabbit skeletal muscle dephosphorylated [ 32 P]phosphorylase kinase. The rate of dephosphorylation was markedly increased by 5–50 μg histone H1/ml. Only the α and α' subunits were dephosphorylated in the absence or presence of histone H1. This is consistent with previous results suggesting that the H1‐stimulated phosphatase is a type‐2 protein phosphatase. The present studies suggest that the histone H1‐stimulation is the result of direct interaction of the histone with the phosphatase.