Götz C, Kartarius S, Scholtes P, Montenarh M
Medical Biochemistry and Molecular Biology, University of the Saarland, Building 44, Homburg, D-66421, Germany.
Biochem Biophys Res Commun. 2000 Feb 24;268(3):882-5. doi: 10.1006/bbrc.2000.2230.
Protein kinase CK2 is a ubiquitous serine/threonine kinase which is involved in many proliferation-related processes in the cell. It is composed of two regulatory beta-subunits and two catalytic alpha-subunits. Its regulation still remains mysterious in spite of many years of intense research. One of its regulators is the cdk inhibitory molecule p21(WAF1)-a protein which is expressed in situations of genotoxic stress. p21(WAF1) binds to the beta-subunit of CK2 and inhibits the activity of CK2. Using deletion mutants of CK2 beta as well as a peptide library consisting of 15-amino-acid-long peptides derived from the polypeptide chain of CK2 beta we mapped the binding region for p21(WAF1) on the polypeptide chain of CK2 beta. We localized an amino-terminal and a carboxy-terminal binding domain. Binding of p21(WAF1) to both regions of the CK2 beta-subunit interferes with the phosphotransferase activity of the CK2 holoenzyme.
蛋白激酶CK2是一种普遍存在的丝氨酸/苏氨酸激酶，参与细胞内许多与增殖相关的过程。它由两个调节性β亚基和两个催化性α亚基组成。尽管经过多年深入研究，其调节机制仍然神秘。其调节因子之一是细胞周期蛋白依赖性激酶抑制分子p21（WAF1）——一种在基因毒性应激情况下表达的蛋白质。p21（WAF1）与CK2的β亚基结合并抑制CK2的活性。利用CK2β的缺失突变体以及由源自CK2β多肽链的15个氨基酸长的肽组成的肽库，我们在CK2β的多肽链上绘制了p21（WAF1）的结合区域。我们定位了一个氨基末端和一个羧基末端结合结构域。p21（WAF1）与CK2β亚基的两个区域结合会干扰CK2全酶的磷酸转移酶活性。
