Interactions of protein kinase CK2β subunit within the holoenzyme and with other proteins

被引:47
|
作者
Kusk, M
Ahmed, R
Thomsen, B
Bendixen, C
Issinger, OG
Boldyreff, B
机构
[1] Odense Univ, Biokem Inst, DK-5230 Odense M, Denmark
[2] Danish Inst Anim Sci, Res Ctr Foulum, Tjele, Denmark
关键词
protein kinase CK2; subunit interaction; two-hybrid screening; p90(rsk); Doc-1; FAF1; IF-2mt; propionyl CoA carboxylase;
D O I
10.1023/A:1006840613986
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Protein kinase CK2 is a ubiquitous, highly conserved protein kinase with a tetrameric alpha(2)beta(2) structure. For the formation of this tetrameric complex a beta-beta dimer seems to be a prerequisite. Using the two-hybrid system and a series of CK2 beta deletion mutants, we mapped domains involved in alpha-beta and beta-beta interactions. We also detected an intramolecular beta interaction within the amino acid stretch 132-165. Using CK2 beta as a bait in a two-hybrid library screening several new putative cellular partners have been identified, among them the S6 kinase p90(rsk), the putative tumor suppressor protein Doc-1, the Pas-associated protein FAF1, the mitochondrial translational initiation factor 2 and propionyl CoA carboxylase beta subunit.
引用
收藏
页码:51 / 58
页数:8
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