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

• Authors: Katarzyna Domańska , Rafał Zieliński , Konrad Kubiński , Ewa Sajnaga , Maciej Masłyk , Maria Bretner , Ryszard Szyszka
• Languages of publication: EN

Abstracts

EN

CK2 is a pleiotropic constitutively active serine/threonine protein kinase composed of two catalytic α- and two regulatory β-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 αα'ββ', α2ββ', α'2ββ', and a free α'-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.

Keywords

EN

protein phosphorylation; isoenzyme specificity; protein kinase CK2; yeast

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2005
• Volume: 52
• Issue: 4
• Pages: 947-951

Dates

published

2005

received

2005-04-21

revised

2005-07-21

accepted

2005-10-11

(unknown)

2005-10-25

Contributors

author

Katarzyna Domańska

• Department of Molecular Biology, Environmental Protection Institute, Catholic University of Lublin, Lublin, Poland

author

Rafał Zieliński

• Department of Molecular Biology, Environmental Protection Institute, Catholic University of Lublin, Lublin, Poland

author

Konrad Kubiński

• Department of Molecular Biology, Environmental Protection Institute, Catholic University of Lublin, Lublin, Poland

author

Ewa Sajnaga

• Department of Molecular Biology, Environmental Protection Institute, Catholic University of Lublin, Lublin, Poland

author

Maciej Masłyk

• Department of Molecular Biology, Environmental Protection Institute, Catholic University of Lublin, Lublin, Poland

author

Maria Bretner

• Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa, Lublin, Poland

author

Ryszard Szyszka

• Department of Molecular Biology, Environmental Protection Institute, Catholic University of Lublin, Lublin, Poland

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