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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2004

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Biochemical and functional characterization of protein kinase CK2 in ascidian Ciona intestinalis oocytes at fertilization. Cloning and sequence analysis of cDNA for alpha and beta subunits

Anno di pubblicazione: 2004

Formato: Elettronico Cartaceo

Autori: Russo GL, Tosto M, Mupo A, Castellano I, Cuomo A, Tosti E.

Affiliazioni autori: Stazione Zoologica Anton Dohrn, Napoli Istituto di Scienze dell'Alimentazione, Consiglio Nazionale delle Ricerche, Avellino

Autori CNR:


Lingua: inglese

Abstract: 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 (alpha and/or alpha') and two regulatory (beta) 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-alpha was catalytically active as a monomer, independently from its regulatory subunit beta; however, CK2-beta was only detectable in unfertilized oocytes where it was associated with a bona fide identified ascidian mitogen-activated protein kinase. After fertilization, CK2-beta was undetectable, suggesting its rapid degradation. Protein sequence analysis of CK2-alpha and -beta cDNA indicated a high identity compared with vertebrate homologs. In addition, the absence of putative phosphorylation sites for Cdc2 kinase on both alpha and beta subunits suggested an important role for CK2 in regulating meiotic cell cycle in C. intestinalis oocytes.

Lingua abstract: inglese

Pagine da: 33012

Pagine a: 23


Journal of biological chemistry American Society for Biochemistry and Molecular Biology
Paese di pubblicazione: Stati Uniti d'America
Lingua: inglese
ISSN: 1083-351X

Numero volume: 279

Referee: Sė: Internazionale

Indicizzato da:

  • Scopus [2-s2.0-3543031609]
  • PubMed [15159401]
  • ISI Web of Science (WOS) [000222849700121]

Altre informazioni: Free access at: http://www.jbc.org/content/279/31/33012.long

Strutture CNR:


Allegati: THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 279, No. 31, pp. 33012-33023, 2004 (application/pdf)

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