title: FtsZ Polymers Tethered to the Membrane by ZipA Are Susceptible to Spatial Regulation by Min Waves.
abstract: Bacterial cell division is driven by an FtsZ ring in which the FtsZ protein localizes at mid-cell and recruits other proteins, forming a divisome. In Escherichia coli, the first molecular assembly of the divisome, the proto-ring, is formed by the association of FtsZ polymers to the cytoplasmic membrane through the membrane-tethering FtsA and ZipA proteins. The MinCDE system plays a major role in the site selection of the division ring because these proteins oscillate from pole to pole in such a way that the concentration of the FtsZ-ring inhibitor, MinC, is minimal at the cell center, thus favoring FtsZ assembly in this region. We show that MinCDE drives the formation of waves of FtsZ polymers associated to bilayers by ZipA, which propagate as antiphase patterns with respect to those of Min as revealed by confocal fluorescence microscopy. The emergence of these FtsZ waves results from the displacement of FtsZ polymers from the vicinity of the membrane by MinCD, which efficiently competes with ZipA for the C-terminal region of FtsZ, a central hub for multiple interactions that are essential for division. The coupling between FtsZ polymers and Min is enhanced at higher surface densities of ZipA or in the presence of crowding agents that favor the accumulation of FtsZ polymers near the membrane. The association of FtsZ polymers to the membrane modifies the response of FtsZ to Min, and comigrating Min-FtsZ waves are observed when FtsZ is free in solution and not attached to the membrane by ZipA. Taken together, our findings show that the dynamic Min patterns modulate the spatial distribution of FtsZ polymers in controlled minimal membranes. We propose that ZipA plays an important role in mid-cell recruitment of FtsZ orchestrated by MinCDE.
authors.affiliation: Max Planck Institute of Biochemistry, Martinsried, Germany.
authors.forename: Ariadna
authors.initials: A
authors.lastname: Martos
authors.affiliation: Max Planck Institute of Biochemistry, Martinsried, Germany; Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.
authors.forename: Ana
authors.initials: A
authors.lastname: Raso
authors.affiliation: Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.
authors.forename: Mercedes
authors.initials: M
authors.lastname: Jiménez
authors.affiliation: Max Planck Institute of Biochemistry, Martinsried, Germany; Institut für Biotechnologie und Bioprozesstechnik, Graz, Austria.
authors.forename: Zdeněk
authors.initials: Z
authors.lastname: Petrášek
authors.affiliation: Centro de Investigaciones Biológicas, CSIC, Madrid, Spain. Electronic address: grivas@cib.csic.es.
authors.forename: Germán
authors.initials: G
authors.lastname: Rivas
authors.affiliation: Max Planck Institute of Biochemistry, Martinsried, Germany. Electronic address: schwille@biochem.mpg.de.
authors.forename: Petra
authors.initials: P
authors.lastname: Schwille
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000737:chemistry / Q000378:metabolism*; D002455:Cell Division; D002462:Cell Membrane / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000166:cytology / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C071525:FtsZ protein, Bacteria; C080466:MinC protein, Bacteria; C103795:ZipA protein, E coli