Conti Joseph, Viola Marissa G, Camberg Jodi L
Department of Cell and Molecular Biology, The University of Rhode Island, Kingston, RI, USA.
Department of Cell and Molecular Biology, The University of Rhode Island, Kingston, RI, USA; Department of Nutrition and Food Sciences, The University of Rhode Island, Kingston, RI, USA.
FEBS Lett. 2015 Jan 16;589(2):201-6. doi: 10.1016/j.febslet.2014.11.047. Epub 2014 Dec 10.
The Min system of proteins, consisting of MinC, MinD and MinE, is essential for normal cell division in Escherichia coli. MinC forms a polar gradient to restrict placement of the division septum to midcell. MinC localization occurs through a direct interaction with MinD, a membrane-associating Par-like ATPase. MinE stimulates ATP hydrolysis by MinD, thereby releasing MinD from the membrane. Here, we show that MinD forms polymers with MinC and ATP without the addition of phospholipids. The topological regulator MinE induces disassembly of MinCD polymers. Two MinD mutant proteins, MinD(K11A) and MinD(ΔMTS15), are unable to form polymers with MinC.
由MinC、MinD和MinE组成的Min蛋白系统对大肠杆菌的正常细胞分裂至关重要。MinC形成极性梯度,将分裂隔膜的位置限制在细胞中部。MinC通过与MinD(一种与膜结合的类Par ATP酶)直接相互作用进行定位。MinE刺激MinD的ATP水解,从而使MinD从膜上释放。在这里,我们表明MinD在不添加磷脂的情况下与MinC和ATP形成聚合物。拓扑调节因子MinE诱导MinCD聚合物的解体。两种MinD突变蛋白MinD(K11A)和MinD(ΔMTS15)不能与MinC形成聚合物。