期刊
NANO LETTERS
卷 18, 期 1, 页码 288-296出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.nanolett.7b04128
关键词
MinD; MinE; pattern formation; atomic force microscopy; cooperativity
类别
资金
- European Research Council (ERC) (MEM-STRUCT-AFM) [310080]
- DFG Collaborative Research Centre Spatiotemporal dynamics of bacterial cells [TRR 174/2017]
- DFG Fellowship through the Graduate School of Quantitative Biosciences Munich (QBM)
The MinDE protein system from E. coli has recently been identified as a minimal biological oscillator, based on two proteins only: The ATPase MinD and the ATPase activating protein MinE. In E. coli, the system works as the molecular ruler to place the divisome at midcell for cell division. Despite its compositional simplicity, the molecular mechanism leading to protein patterns and oscillations is still insufficiently understood. Here we used highspeed atomic force microscopy to analyze the mechanism of MinDE membrane association/dissociation dynamics on isolated membrane patches, down to the level of individual point oscillators. This nanoscale analysis shows that MinD association to and dissociation from the membrane are both highly cooperative but mechanistically different processes. We propose that they represent the two directions of a single allosteric switch leading to MinD filament formation and depolymerization. Association/dissociation are separated by rather long apparently silent periods. The membrane-associated period is characterized by MinD filament multivalent binding, avidity, while the dissociated period is defined by seeding of individual MinD. Analyzing association/dissociation kinetics with varying MinD and MinE concentrations and dependent on membrane patch size allowed us to disentangle the essential dynamic variables of the MinDE oscillation cycle.
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