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Molecular evolution of the metazoan protein kinase C multigene family

Kruse, Michael; Gamulin, Vera; Ćetković, Helena; Pancer, Zev; Mueller, Isabel M.; Mueller, Werner E.G.
Molecular evolution of the metazoan protein kinase C multigene family // Journal of molecular evolution, 43 (1996), 4; 374-383 doi:10.1007/BF02339011 (međunarodna recenzija, članak, znanstveni)

Molecular evolution of the metazoan protein kinase C multigene family

Kruse, Michael ; Gamulin, Vera ; Ćetković, Helena ; Pancer, Zev ; Mueller, Isabel M. ; Mueller, Werner E.G.

Journal of molecular evolution (0022-2844) 43 (1996), 4; 374-383

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Sponges ; Geodia cydonium ; serine/threonine kinases ; phylogeny ; molecular systematics ; molecular evolution

Protein kinases C (PKCs) comprise closely related Ser/Thr kinases, ubiquitously present in animal tissues ; they respond to second messengers, e.g., Ca2+ and/or diacylglycerol, to express their activities. Two PKCs have been sequenced from Geodia cydonium, a member of the lowest multicellular animals, the sponges (Porifera). One sponge G. cydonium PKC, GCPKC1, belongs to the ''novel'' (Ca2+-independent) PKC (nPKC) subfamily while the second one, GCPKC2, has the hall-marks of the ''conventional'' (Ca2+-dependent) PKC (cPKC) subfamily. The alignment of the Ser/Thr catalytic kinase domains, of the predicted aa sequences for these cDNAs with respective segments from previously reported sequences, revealed highest homology to PKCs from animals but also distant relationships to Ser/Thr kinases from protozoa, plants, and bacteria. However, a comparison of the complete structures of the sponge PKCs, which are-already-identical to those of nPKCs and cPKCs from higher metazoa, with the structures of protozoan, plant, and bacterial Ser/Thr kinases indicates that the metazoan PKCs have to be distinguished from the nonmetazoan enzymes. These data indicate that metazoan PKCs have a universal common ancestor which they share with the nonmetazoan Ser/Thr kinases with respect to the kinase domain, but they differ from them in overall structural composition.

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Projekt / tema

Institut "Ruđer Bošković", Zagreb

Časopis indeksira:

  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus