MinE conformational switching confers robustness on self-organized Min protein patterns

Area of Science:

• Cellular processes
• Protein patterning
• Bacterial cell division

Background:

• Protein patterning is crucial for cellular functions.
• The bacterial Min system exhibits self-organized oscillations for cell division.
• MinE's conformational switch is proposed but its role is unclear.

Purpose of the Study:

• Investigate the functional relevance of MinE's conformational switch.
• Determine the role of MinE's switch in Min network pattern formation.
• Understand how molecular details contribute to robust protein patterning.

Main Methods:

• Mathematical modeling of the Min system.
• In vitro reconstitution using mutant proteins.
• Dissecting MinE's membrane binding and MinD affinity changes.

Main Results:

• MinD-dependent change in MinE's affinity for MinD is essential for pattern emergence.
• This mechanism ensures pattern formation across a physiological range of protein concentrations.
• Conformational switching spatially separates functional states of ATPase-activating proteins.

Conclusions:

• MinE's switch, specifically altered affinity for MinD, is critical for robust Min system oscillations.
• Conformational switching in ATPase-activating proteins can create robust intracellular networks.
• This mechanism provides insights into the fundamental principles of protein patterning in bacteria.