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

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.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Hsieh CW,Lin TY,Lai HM,Lin CC,Hsieh TS,Shih YL

doi

10.1111/j.1365-2958.2009.07006.x

subject

Has Abstract

pub_date

2010-01-01 00:00:00

pages

499-512

issue

2

eissn

0950-382X

issn

1365-2958

pii

MMI7006

journal_volume

75

pub_type

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