title: GTPase activity-coupled treadmilling of the bacterial tubulin FtsZ organizes septal cell wall synthesis.
abstract: The bacterial tubulin FtsZ is the central component of the cell division machinery, coordinating an ensemble of proteins involved in septal cell wall synthesis to ensure successful constriction. How cells achieve this coordination is unknown. We found that inEscherichia colicells, FtsZ exhibits dynamic treadmilling predominantly determined by its guanosine triphosphatase activity. The treadmilling dynamics direct the processive movement of the septal cell wall synthesis machinery but do not limit the rate of septal synthesis. In FtsZ mutants with severely reduced treadmilling, the spatial distribution of septal synthesis and the molecular composition and ultrastructure of the septal cell wall were substantially altered. Thus, FtsZ treadmilling provides a mechanism for achieving uniform septal cell wall synthesis to enable correct polar morphology.
authors.affiliation: Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
authors.forename: Xinxing
authors.identifier: 0000-0002-2101-9881
authors.initials: X
authors.lastname: Yang
authors.affiliation: Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
authors.forename: Zhixin
authors.identifier: 0000-0001-7668-614X
authors.initials: Z
authors.lastname: Lyu
authors.affiliation: Department of Bioengineering, Stanford University, Stanford, CA 94305, USA.
authors.forename: Amanda
authors.identifier: 0000-0003-2750-4842
authors.initials: A
authors.lastname: Miguel
authors.affiliation: Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
authors.forename: Ryan
authors.identifier: 0000-0002-0399-5248
authors.initials: R
authors.lastname: McQuillen
authors.affiliation: Department of Bioengineering, Stanford University, Stanford, CA 94305, USA. kchuang@stanford.edu xiao@jhmi.edu.|Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.
authors.forename: Kerwyn Casey
authors.identifier: 0000-0002-8043-8138
authors.initials: KC
authors.lastname: Huang
authors.affiliation: Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. kchuang@stanford.edu xiao@jhmi.edu.
authors.forename: Jie
authors.identifier: 0000-0003-1433-5437
authors.initials: J
authors.lastname: Xiao
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism* / Q000648:ultrastructure; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000648:ultrastructure; D020558:GTP Phosphohydrolases / Q000235:genetics / Q000378:metabolism*; D006868:Hydrolysis; D009154:Mutation; D010457:Peptidoglycan / Q000096:biosynthesis; D014404:Tubulin / Q000235:genetics / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D010457:Peptidoglycan; D014404:Tubulin; D020558:GTP Phosphohydrolases