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J. Biochem, 1993, Vol. 113, No. 3 334-342
© 1993 Japanese Biochemical Society

research-article

Characterization of Casein Kinase II, and of p98 as One of Its Effective Phosphate Acceptors in Sea Urichin Eggs1

Kenzo Ohtsuki*,2, Masahiro Matsumoto*, Hitoshi Saito* and Tokyoki Kato**

*Laboratory of Genetical Biochemistry, Department of Bioscience, Kitasato Universisty School of Hygenic Sciences Sagamihara, Kanagawa 228
**Sugashima Marine Biological Laboratory, Nagoya Univeristy Toba, Mie 517

2To whom correspondence should be addressed.

CK-II has been partially purified from a 1.5 M KC1 extract of unfertilized sea urchin eggs by means of DEAE-cellulose column chromatography, gel filtration on Sephacryl S300, and heparin-agarose column chromatography, successively. This partially purified CK-II was associated with a 98 kDa polypeptide (designated as p98), which was then separated from the kinase by Mono Q column chromatography (HPLC). The biochemical characteristics of CK-II purified from unfertilized eggs were similar to those of CK-IIs from various mammalian cells: requirements of divalent cations (Mg2+ and Mn2+) and phosphate acceptors (casein and p98), response to basic polypeptides and heparin, subunit structure and molecular size. Moreover, it was found that (i) p98 (apparent pi 10.0) has DNA-binding ability and functions as an effective phosphate acceptor for CK-II in vitro; (ii) phosphorylation of p98 by the kinase was highly stimulated by histone-like sperm protein from sea urchin sperm, protamine (salmon sperm), and poly Arg; and (iii) selective phosphorylation of p98 by CK-II was detected when the DEAE-cellulose fraction from unfertilized eggs was incubated with [ r-32P] ATP in the presence of protamine. Some biochemical characteristics of p98 from the eggs were similar to those of transcriptional factor Spl. The evidence obtained suggests that (i) arginine-rich sperm proteins function as potent activators for CK-II in unfertilized eggs and (ii) specific phosphorylation of p98 by the activated kinase may play an important role in the transcriptional regulation in the eggs accompanying fertilization.

1This work was supported in part by grants from Ministry of Education Sciences and Culture of Japan (Grant-in-Aid No.02808030, 1991) and from the Research Foundation of the Japan Private School Association (1992).


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