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直接的 MinE-膜相互作用有助于 MinDE 在大肠杆菌中的正确定位。

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

机构信息

Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei, Taiwan.

出版信息

Mol Microbiol. 2010 Jan;75(2):499-512. doi: 10.1111/j.1365-2958.2009.07006.x. Epub 2009 Dec 16.

DOI:10.1111/j.1365-2958.2009.07006.x
PMID:20025670
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2814086/
Abstract

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.

摘要

大肠杆菌 Min 系统的动态振荡决定了细胞分裂平面的位置在细胞中部。除了刺激 MinD ATP 酶活性外,我们在此报告 MinE 可以直接与膜相互作用,并且这种相互作用有助于 MinDE 的正确定位和动力学。MinE 的 N 端结构域参与 MinE 与膜之间的直接接触,随后可能由 MinE 的 C 端结构域稳定。在体外系统中,MinE 导致脂质体变形为膜管,其性质类似于先前报道的 MinD。我们分离到一个突变 MinE,其包含 R10、K11 和 K12 残基的取代,完全能够刺激 MinD ATP 酶活性,但在膜结合方面存在缺陷。重要的是,这种突变体不能支持正常的 MinDE 定位和振荡,这表明 MinE 与膜的直接相互作用对于 Min 系统的动态行为至关重要。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73ec/2814086/e2cf841000e5/mmi0075-0499-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73ec/2814086/928056540e53/mmi0075-0499-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73ec/2814086/ce6bdaadf7cb/mmi0075-0499-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73ec/2814086/d8e7014e9148/mmi0075-0499-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73ec/2814086/739ae8cb0c79/mmi0075-0499-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73ec/2814086/2489f42ba2d5/mmi0075-0499-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73ec/2814086/e2cf841000e5/mmi0075-0499-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73ec/2814086/928056540e53/mmi0075-0499-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73ec/2814086/ce6bdaadf7cb/mmi0075-0499-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73ec/2814086/d8e7014e9148/mmi0075-0499-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73ec/2814086/739ae8cb0c79/mmi0075-0499-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73ec/2814086/2489f42ba2d5/mmi0075-0499-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73ec/2814086/e2cf841000e5/mmi0075-0499-f6.jpg

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