title: Robust Min-system oscillation in the presence of internal photosynthetic membranes in cyanobacteria.
abstract: The oscillatory Min system of Escherichia coli defines the cell division plane by regulating the site of FtsZ-ring formation and represents one of the best-understood examples of emergent protein self-organization in nature. The oscillatory patterns of the Min-system proteins MinC, MinD and MinE (MinCDE) are strongly dependent on the geometry of membranes they bind. Complex internal membranes within cyanobacteria could disrupt this self-organization by sterically occluding or sequestering MinCDE from the plasma membrane. Here, it was shown that the Min system in the cyanobacterium Synechococcus elongatus PCC 7942 oscillates from pole-to-pole despite the potential spatial constraints imposed by their extensive thylakoid network. Moreover, reaction-diffusion simulations predict robust oscillations in modeled cyanobacterial cells provided that thylakoid network permeability is maintained to facilitate diffusion, and suggest that Min proteins require preferential affinity for the plasma membrane over thylakoids to correctly position the FtsZ ring. Interestingly, in addition to oscillating, MinC exhibits a midcell localization dependent on MinD and the DivIVA-like protein Cdv3, indicating that two distinct pools of MinC are coordinated in S. elongatus. Our results provide the first direct evidence for Min oscillation outside of E. coli and have broader implications for Min-system function in bacteria and organelles with internal membrane systems.
authors.affiliation: Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI, 48824, USA.
authors.forename: Joshua S
authors.initials: JS
authors.lastname: MacCready
authors.affiliation: Department of Computer Science, Michigan State University, East Lansing, MI, 48824, USA.
authors.forename: Jory
authors.initials: J
authors.lastname: Schossau
authors.affiliation: Department of Plant Biology, Michigan State University, East Lansing, MI, 48824, USA.
authors.forename: Katherine W
authors.initials: KW
authors.lastname: Osteryoung
authors.affiliation: Department of Biochemistry, MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI, 48824, USA.
authors.forename: Daniel C
authors.initials: DC
authors.lastname: Ducat
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology*; D018797:Cell Cycle Proteins / Q000378:metabolism; D002455:Cell Division; D002462:Cell Membrane / Q000378:metabolism; D003198:Computer Simulation; D000458:Cyanobacteria / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology*; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D013329:Structure-Activity Relationship; D046940:Synechococcus / Q000378:metabolism* / Q000502:physiology; D020524:Thylakoids / Q000502:physiology
chemical_list: D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C071525:FtsZ protein, Bacteria; D008565:Membrane Proteins; D000251:Adenosine Triphosphatases