Abstract
The 60S ribosomes from Saccharomyces cerevisiae contain a set of acidic P-proteins playing an important role in the ribosome function. Reversible phosphorylation of those proteins is a mechanism regulating translational activity of ribosomes. The key role in regulation of this process is played by specific, second messenger-independent protein kinases. The PK60S kinase was one of the enzymes phosphorylating P-proteins. The enzyme has been purified from yeast and characterised. Pure enzyme has properties similar to those reported for casein kinase type 2. Peptide mass fingerprinting (PMF) has identified the PK60S as a catalytic α′ subunit of casein kinase type 2 (CK2α′). Protein kinase activity is inhibited by SOD1 and by highly specific CK2 inhibitor - 4,5,6,7-tetrabromo-benzotriazole (TBBt). The possible mechanism of regulation of CK2α′ activity in stress conditions, by superoxide dismutase in regulation of 80S-ribosome activity, is discussed.
Original language | English (US) |
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Pages (from-to) | 31-40 |
Number of pages | 10 |
Journal | Biochemical and biophysical research communications |
Volume | 307 |
Issue number | 1 |
DOIs | |
State | Published - Jul 18 2003 |
Externally published | Yes |
Keywords
- CK2α′
- P1/P2 proteins
- Protein kinases
- Ribosome phosphorylation
- SOD1
- Yeast
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology