Different properties of four molecular forms of protein kinase CK2 from Saccharomyces cerevisiae. | Zendy

Katarzyna Domańska | Zendy; Rafał Zieliński | Zendy; Konrad Kubiński | Zendy; Ewa Sajnaga | Zendy; Maciej Masłyk | Zendy; Maria Bretner | Zendy; Ryszard Szyszka | Zendy

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Different properties of four molecular forms of protein kinase CK2 from Saccharomyces cerevisiae.

Author(s) -

Katarzyna Domańska,

Rafał Zieliński,

Konrad Kubiński,

Ewa Sajnaga,

Maciej Masłyk,

Maria Bretner,

Ryszard Szyszka

Publication year - 2005

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2005_3413

Subject(s) - protein subunit , saccharomyces cerevisiae , yeast , threonine , serine , casein kinase 2 , biochemistry , protein kinase a , alpha (finance) , kinase , chemistry , phosphorylation , biology , microbiology and biotechnology , gene , cyclin dependent kinase 2 , medicine , construct validity , nursing , patient satisfaction

CK2 is a pleiotropic constitutively active serine/threonine protein kinase composed of two catalytic alpha- and two regulatory beta-subunits, whose regulation is still not well understood. It seems to play an essential role in regulation of many cellular processes. Four active forms of CK2, composed of alphaalpha'betabeta', alpha(2)betabeta', alpha'(2)betabeta', and a free alpha'-subunit were isolated from wild-type yeast and strains containing a single deletion of the catalytic subunit. Each species exhibits properties typical for CK2, but they differ in substrate specificity and sensitivity to inhibitors. This suggests that each CK2 isomer may regulate different process or may differ in the way of its regulation.

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