Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli

被引:73
作者
Hsieh, Cheng-Wei [1 ]
Lin, Ti-Yu [1 ]
Lai, Hsin-Mei [1 ,2 ]
Lin, Chu-Chi [1 ]
Hsieh, Ting-Sung [1 ,2 ]
Shih, Yu-Ling [1 ,2 ]
机构
[1] Acad Sinica, Inst Biol Chem, Taipei 115, Taiwan
[2] Natl Taiwan Univ, Inst Biochem Sci, Taipei 106, Taiwan
关键词
DIVISION SITE SELECTION; ESCHERICHIA-COLI; CELL-DIVISION; PLACEMENT; ATPASE; STIMULATION; OSCILLATION; MUTATIONS; RESIDUES; BINDING;
D O I
10.1111/j.1365-2958.2009.07006.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Dynamic oscillation of the Min system in Escherichia coli determines the placement of the division plane at the midcell. In addition to stimulating MinD ATPase activity, we report here that MinE can directly interact with the membrane and this interaction contributes to the proper MinDE localization and dynamics. The N-terminal domain of MinE is involved in direct contact between MinE and the membranes that may subsequently be stabilized by the C-terminal domain of MinE. In an in vitro system, MinE caused liposome deformation into membrane tubules, a property similar to that previously reported for MinD. We isolated a mutant MinE containing residue substitutions in R10, K11 and K12 that was fully capable of stimulating MinD ATPase activity, but was deficient in membrane binding. Importantly, this mutant was unable to support normal MinDE localization and oscillation, suggesting that direct MinE interaction with the membrane is critical for the dynamic behavior of the Min system.
引用
收藏
页码:499 / 512
页数:14
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