Ma Lu-Yan, King Glenn, Rothfield Lawrence
Department of Microbiology, University of Connecticut Health Center, Farmington, Connecticut 06032, USA.
J Bacteriol. 2003 Aug;185(16):4948-55. doi: 10.1128/JB.185.16.4948-4955.2003.
Interactions between the MinD and MinE proteins are required for proper placement of the Escherichia coli division septum. The site within MinE that is required for interaction with MinD was mapped by studying the effects of site-directed minE mutations on MinD-MinE interactions in yeast two-hybrid and three-hybrid experiments. This confirmed that the MinE N-terminal domain is responsible for the interaction of MinE with MinD. Mutations that interfered with the interaction defined an extended surface on one face of the alpha-helical region of the MinE N-terminal domain, consistent with the idea that the MinE-MinD interaction involves formation of a coiled-coil structure by interaction with a complementary helical surface within MinD.
MinD蛋白与MinE蛋白之间的相互作用对于大肠杆菌分裂隔膜的正确定位是必需的。通过研究定点诱变的minE突变对酵母双杂交和三杂交实验中MinD-MinE相互作用的影响,确定了MinE中与MinD相互作用所需的位点。这证实了MinE的N端结构域负责MinE与MinD的相互作用。干扰这种相互作用的突变在MinE N端结构域α螺旋区域的一个面上定义了一个延伸的表面,这与MinE-MinD相互作用涉及通过与MinD内互补螺旋表面相互作用形成卷曲螺旋结构的观点一致。