The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis

作者：Park Kyung Tae; Wu Wei; Battaile Kevin P; Lovell Scott; Holyoak Todd; Lutkenhaus Joe^*

来源：Cell, 2011, 146(3): 396-407.

DOI：10.1016/j.cell.2011.06.042

In E. coli, MinD recruits MinE to the membrane, leading to a coupled oscillation required for spatial regulation of the cytokinetic Z ring. How these proteins interact, however, is not clear because the MinD-binding regions of MinE are sequestered within a six-stranded beta sheet and masked by N-terminal helices. minE mutations that restore interaction between some MinD and MinE mutants were isolated. These mutations alter the MinE structure leading to release of the MinD-binding regions and the N-terminal helices that bind the membrane. Crystallization of MinD-MinE complexes revealed a four-stranded beta sheet MinE dimer with the released beta strands (MinD-binding regions) converted to alpha helices bound to MinD dimers. These results identify the MinD-dependent conformational changes in MinE that convert it from a latent to an active form and lead to a model of how MinE persists at the MinD-membrane surface.

• 出版日期2011-8-5