The protein kinase 60S is a free catalytic CK2alpha' subunit and forms an inactive complex with superoxide dismutase SOD1

• 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 alpha(') subunit of casein kinase type 2 (CK2alpha(')). 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 CK2alpha(') activity in stress conditions, by superoxide dismutase in regulation of 80S-ribosome activity, is discussed.

Nyckelord

Casein Kinase II

Catalytic Domain

DNA-Binding Proteins/genetics/isolation & purification/metabolism

Fungal Proteins/genetics/*metabolism

Multienzyme Complexes

Peptides/genetics/metabolism

Phosphorylation

Protein Isoforms/genetics/metabolism

Protein-Serine-Threonine Kinases/genetics/isolation & purification/*metabolism

Ribosomes/metabolism

Saccharomyces cerevisiae/*enzymology/metabolism

Superoxide Dismutase/*metabolism

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