Higashitani A, Higashitani N, Horiuchi K
Department of Microbial Genetics, National Institute of Genetics, Mishima, Japan.
Biochem Biophys Res Commun. 1995 Apr 6;209(1):198-204. doi: 10.1006/bbrc.1995.1489.
E. coli SulA is an SOS-inducible protein that inhibits cell division. FtsZ is a protein that plays a central role in bacterial cell division. Using purified SulA protein that was fused to the maltose binding protein, we demonstrate in vitro that SulA interacts with FtsZ to form a stable complex. The reaction requires GTP and Mg ion. GDP and GTP gamma S cannot substitute for GTP, which suggests that hydrolysis of GTP is required for the reaction. The complex is formed in a molar ratio of approximately one to one of the two proteins. It is likely that the complex formation represents the in vivo mechanism by which SulA inhibits cell division.
大肠杆菌SulA是一种SOS诱导蛋白，可抑制细胞分裂。FtsZ是一种在细菌细胞分裂中起核心作用的蛋白质。我们使用与麦芽糖结合蛋白融合的纯化SulA蛋白，在体外证明SulA与FtsZ相互作用形成稳定复合物。该反应需要GTP和镁离子。GDP和GTPγS不能替代GTP，这表明该反应需要GTP水解。复合物以两种蛋白质大约一对一的摩尔比形成。复合物的形成很可能代表了SulA在体内抑制细胞分裂的机制。
