Karimova G, Ullmann A, Ladant D
Unité de Biochimie Cellulaire, CNRS URA 2185, Institut Pasteur, Paris, France.
Int J Med Microbiol. 2000 Oct;290(4-5):441-5. doi: 10.1016/S1438-4221(00)80060-0.
Bordetella pertussis secretes a calmodulin-activated adenylate cyclase toxin (CyaA) that is able to enter into eukaryotic cells. We took advantage of the modular structure of the catalytic domain of CyaA to design a genetic system that can detect protein-protein interactions in Escherichia coli. This bacterial two-hybrid system is based on the functional complementation between two complementary fragments, T25 and T18, of the catalytic domain of CyaA, in an E. coli cya strain. This bacterial two-hybrid system could find applications in the studies of structure/function relationships of proteins, in functional analysis of genomes, in high-throughput screening of interacting ligands and in design of new therapeutic agents.
百日咳博德特氏菌分泌一种能够进入真核细胞的钙调蛋白激活腺苷酸环化酶毒素（CyaA）。我们利用CyaA催化结构域的模块化结构设计了一种可在大肠杆菌中检测蛋白质-蛋白质相互作用的遗传系统。这种细菌双杂交系统基于CyaA催化结构域的两个互补片段T25和T18在大肠杆菌cya菌株中的功能互补。该细菌双杂交系统可应用于蛋白质结构/功能关系研究、基因组功能分析、相互作用配体的高通量筛选以及新型治疗药物的设计。
