Boldyreff B, Issinger O G
Biokemisk Institut, Odense Universitet, Denmark.
FEBS Lett. 1997 Feb 17;403(2):197-9. doi: 10.1016/s0014-5793(97)00010-0.
In a search for protein kinase CK2 beta subunit binding proteins using the two-hybrid system, more than 1000 positive clones were isolated. Beside clones for the alpha' and beta subunit of CK2, there were clones coding for a so far unknown protein, whose partial cDNA sequence was already deposited in the EMBL database under the accession numbers R08806 and Z17360, for the ribosomal protein L5 and for A-Raf kinase. All isolated clones except the one for CK2 beta showed no interaction with the catalytic alpha subunit of CK2. A-Raf kinase is a new interesting partner of CK2 beta. The isolated A-Raf clone represented amino acids 268-606, but also a full length A-Raf clone interacted with CK2 beta. At the site of CK2 beta, residue 175 and amino acids between residues 194 and 200 are likely to be involved in direct interaction.
在利用双杂交系统寻找蛋白激酶CK2β亚基结合蛋白的过程中，分离出了1000多个阳性克隆。除了CK2α'和β亚基的克隆外，还有一些克隆编码一种迄今未知的蛋白质，其部分cDNA序列已以登录号R08806和Z17360存入EMBL数据库，另外还有核糖体蛋白L5和A-Raf激酶的克隆。除CK2β的克隆外，所有分离出的克隆均未与CK2的催化α亚基发生相互作用。A-Raf激酶是CK2β一个新的有趣的相互作用伙伴。分离出的A-Raf克隆代表第268至606位氨基酸，但全长A-Raf克隆也能与CK2β相互作用。在CK2β位点，第175位残基以及第194至200位残基之间的氨基酸可能参与直接相互作用。
