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The protein kinase 60S is a free catalytic CK2alpha' subunit and forms an inactive complex with superoxide dismutase SOD1
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2003 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 307, no 1, 31-40 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2003. Vol. 307, no 1, 31-40 p.
Keyword [en]
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
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-10343DOI: 10.1016/S0006-291X(03)01126-4PubMedID: 12849977OAI: oai:DiVA.org:uu-10343DiVA: diva2:38111
Available from: 2007-03-16 Created: 2007-03-16 Last updated: 2013-10-03Bibliographically approved

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Publisher's full textPubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=12849977&dopt=Citation

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