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 Microbioljournal_title
Molecular microbiologyauthors
Hsieh CW,Lin TY,Lai HM,Lin CC,Hsieh TS,Shih YLdoi
10.1111/j.1365-2958.2009.07006.xsubject
Has Abstractpub_date
2010-01-01 00:00:00pages
499-512issue
2eissn
0950-382Xissn
1365-2958pii
MMI7006journal_volume
75pub_type
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