Phosphorylation of calf thymus H1 histone by calcium-activated, phospholipid-dependent protein kinase
Biochemical and Biophysical Research CommunicationsPublished 1 September 1980
Yasushi Iwasa, Yoshimi Takai, Ushio Kikkawa, Yasutomi Nishizuka
Citations65
SJR quartileQ2
SJR score0.75
SNIP0.56
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TL;DR
Analysis on the N-bromosuccinimide-bisected fragments of this radioactive histone has revealed that the enzyme phosphorylates preferentially seryl and threonyl residues located in the carboxyl-terminal half of this histone molecule.
Abstract
Ca2+-activated, phospholipid-dependent protein kinase recently found in mammalian tissues (Takai, Y., Kishimoto, A., Iwasa, Y., Kawahara, Y., Mori, T., and Nishizuka, Y. (1979) J.Biol.Chem.254, 3692–3695) is able to phosphorylate five fractions of calf thymus histone. H1 histone serves as a preferential substrate, and approximately two moles of phosphate are incorporated into every mole of this histone. Analysis on the N-bromosuccinimide-bisected fragments of this radioactive histone has revealed that the enzyme phosphorylates preferentially seryl and threonyl residues located in the carboxyl-terminal half of this histone molecule.
Keywords
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