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Direct MinE–membrane interaction contributes to the proper localization of MinDE in E. coli
Author(s) -
Hsieh ChengWei,
Lin TiYu,
Lai HsinMei,
Lin ChuChi,
Hsieh TingSung,
Shih YuLing
Publication year - 2010
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2009.07006.x
Subject(s) - mutant , membrane , biology , effector , microbiology and biotechnology , biophysics , oscillation (cell signaling) , atpase , escherichia coli , residue (chemistry) , biochemistry , gene , enzyme
Summary 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.