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MinC/MinD copolymers are not required for Min function.

Kyung-Tae Park¹, Shishen Du¹, Joe Lutkenhaus¹

¹Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, KS, 66160, USA.

Molecular Microbiology

|August 14, 2015

Summary

This summary is machine-generated.

Bacterial cell division relies on Min proteins to position the Z ring correctly. This study shows MinC/MinD copolymer formation is not essential for spatial regulation, challenging previous models.

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In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers

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Area of Science:

Microbiology
Cell Biology
Biochemistry

Background:

Precise placement of the Z ring during cell division in Escherichia coli is regulated by the Min proteins (MinC, MinD, and MinE).
MinD activates MinC, an FtsZ inhibitor, by recruiting it to the membrane and Z ring.
MinE stimulates MinD's ATPase activity, creating oscillations that exclude MinC/MinD from midcell.

Purpose of the Study:

To investigate the role of MinC/MinD copolymer formation in the spatial regulation of the Z ring.
To determine if MinC/MinD copolymerization is a prerequisite for the inhibitory activity of MinC on FtsZ.

Main Methods:

Utilized MinD mutants defective in MinC binding to create heterodimers unable to form MinC/MinD copolymers.
Generated heterodimers using MinC mutants defective in MinD binding.
Assessed the activity and spatial regulatory function of these non-copolymerizing heterodimers.

Main Results:

Heterodimers formed from MinC or MinD mutants defective in binding were active.
These active heterodimers were capable of mediating spatial regulation of the Z ring.
Demonstrated that MinC/MinD copolymer formation is not required for Z ring spatial regulation.

Conclusions:

MinC/MinD copolymerization is not essential for the spatial control of cell division in E. coli.
Supports a model where membrane-anchored MinC/MinD complexes target the Z ring via FtsZ's C-terminus, leading to FtsZ filament disruption.