ISSN:
1573-4919
Keywords:
protein kinase CK2
;
subunit interaction
;
two-hybrid screening
;
p90rsk
;
Doc-1
;
FAF1
;
IF-2mt
;
propionyl CoA carboxylase
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
Abstract Protein kinase CK2 is a ubiquitous, highly conserved protein kinase with a tetrameric α2β2 structure. For the formation of this tetrameric complex a β-β dimer seems to be a prerequisite. Using the two-hybrid system and a series of CK2β deletion mutants, we mapped domains involved in α-β and β-β interactions. We also detected an intramolecular b interaction within the amino acid stretch 132-165. Using CK2β as a bait in a two-hybrid library screening several new putative cellular partners have been identified, among them the S6 kinase p90rsk, the putative tumor suppressor protein Doc-1, the Fas-associated protein FAF1, the mitochondrial translational initiation factor 2 and propionyl CoA carboxylase β subunit.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1006840613986
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