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J. Biol. Chem., Vol. 279, Issue 31, 33012-33023, July 30, 2004

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Biochemical and Functional Characterization of Protein Kinase CK2 in Ascidian Ciona intestinalis Oocytes at Fertilization

CLONING AND SEQUENCE ANALYSIS OF cDNA FOR AND SUBUNITS^*

Gian Luigi Russo¶, Mariarosaria Tosto, Annalisa Mupo, Immacolata Castellano, Annunziata Cuomo, and Elisabetta Tosti

From the Stazione Zoologica Anton Dohrn, Napoli 80121 and the Istituto di Scienze dell'Alimentazione, Consiglio Nazionale delle Ricerche, Avellino 83100, Italy

The ubiquitous and pleiotropic dual specificity protein kinase CK2 has been studied and characterized in many organisms, from yeast to mammals. Generally, the enzyme is composed of two catalytic ( and/or ') and two regulatory () subunits, forming a differently assembled tetramer. Although prone to controversial interpretation, the function of CK2 has been associated with fundamental biological processes such as signal transduction, cell cycle progression, cell growth, apoptosis, and transcription. Less known is the role of CK2 during meiosis and the early phase of embryogenesis. In this work, we studied CK2 activity during oocyte activation, a process occurring at the end of oocyte maturation and triggered by fertilization. In ascidian Ciona intestinalis, an organism whose complete genome has been published recently, CK2 was constitutively active in unfertilized and fertilized oocytes. The enzymatic activity oscillated through meiosis showing three major peaks: soon after fertilization (metaphase I exit), before metaphase II, and at the exit from metaphase II. Biochemical analysis of CK2 subunit composition in activated oocytes indicated that CK2- was catalytically active as a monomer, independently from its regulatory subunit ; however, CK2- was only detectable in unfertilized oocytes where it was associated with a bona fide identified ascidian mitogen-activated protein kinase. After fertilization, CK2- was undetectable, suggesting its rapid degradation. Protein sequence analysis of CK2- and - cDNA indicated a high identity compared with vertebrate homologs. In addition, the absence of putative phosphorylation sites for Cdc2 kinase on both and subunits suggested an important role for CK2 in regulating meiotic cell cycle in C. intestinalis oocytes.

Received for publication, January 30, 2004 , and in revised form, April 19, 2004.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY092081 (CiCK2A) and AF360544 (CiCK2B).

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed: Istituto di Scienze dell'Alimentazione, Via Roma 52 A/C, Avellino 83100, Italy. Tel.: 39-0825-299-431; Fax: 39-0825-781-585; E-mail: glrusso{at}szn.it.

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