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PMID: 2177468 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Histone H1 kinase specific to the SPKK motif.

Journal of biochemistry ·Vol. 108 ·No. 3 ·1990-09-00 ·Pages 356-64

Suzuki M, Sohma H, Yazawa M, Yagi K, Ebashi S

Abstract

A protein kinase phosphorylating sea urchin spermatogenous histones, H1 and H2B, was found in sea urchin egg homogenate and purified. The kinase is activated by cAMP and is composed of two different types of subunits with molecular masses 41 and 46 kDa. The kinase phosphorylates a peptide, Ser-Pro-Arg-Lys-Ser-Pro-Arg-Lys, which is a double repeat of the DNA-binding SPKK motif [Suzuki M., (1989) EMBO J. 8, 797-804]. We name this kinase SPkinase because it exclusively phosphorylates H1 and H2B, the only histones containing SPKK motifs. Phosphorylation of H1 by SPkinase decreases the DNA-binding ability of H1. This paper is the first to report purification of a kinase which affects the DNA-binding ability of a gene regulatory protein.

MeSH Terms
Amino Acid Sequence Animals Chromatography, Affinity Cyclic AMP/pharmacology DNA-Binding Proteins Enzyme Activation/drug effects Histones/metabolism Male Maturation-Promoting Factor/chemistry,metabolism Molecular Sequence Data Ovum/drug effects,enzymology Phosphorylation Protein Conformation Sea Urchins Spermatozoa/drug effects,enzymology Substrate Specificity
Chemicals
DNA-Binding Proteins Histones Cyclic AMP Maturation-Promoting Factor
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Suzuki M
National Institute for Physiological Sciences, Aichi.
Sohma H
Yazawa M
Yagi K
Ebashi S
Article Info
Journal
Journal of biochemistry
Abbr.
J Biochem
ISSN
0021-924X
Published
1990-09-00
Pages
356-64
Language
English
Region
England
NLM ID
0376600
Subset
IM
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