The relationship between hetero-oligomer formation and function of the topological specificity domain of the Escherichia coli MinE protein.
The relationship between hetero-oligomer formation and function of the topological specificity domain of the Escherichia coli MinE protein.
复制标题
异源寡聚物形成与大肠杆菌 MinE 蛋白拓扑特异性结构域功能之间的关系。
DOI:
10.1046/j.1365-2958.1998.01059.x
复制
发表时间:
1998
影响因子:
3.6
通讯作者:
Rothfield,L
中科院分区:
文献类型:
--
作者:
Zhang,Y;Rowland,S;King,G;Braswell,E;Rothfield,L
MinE is an oligomeric protein that, in conjunction with other Min proteins, is required for the proper placement of the cell division site ofEscherichia coli. We have examined the self‐association properties of MinE by analytical ultracentrifugation and by studies of hetero‐oligomer formation in non‐denaturing polyacrylamide gels. The self‐association properties of purified MinE predict that cytoplasmic MinE is likely to exist as a mixture of monomers and dimers. Consistent with this prediction, the C‐terminal MinE22–88fragment forms hetero‐oligomers with MinE+when the proteins are co‐expressed. In contrast, the MinE36–88fragment does not form MinE+/MinE36–88hetero‐oligomers, although MinE36–88affects the topological specificity of septum placement as shown by its ability to induce minicell formation when co‐expressed with MinE+in wild‐type cells. Therefore, hetero‐oligomer formation is not necessary for the induction of minicelling by expression of MinE36–88in wild‐type cells. The interference with normal septal placement is ascribed to competition between MinE36–88and the corresponding domain in the complete MinE protein for a component required for the topological specificity of septal placement.