title: Three mutations in Escherichia coli that generate transformable functional flagella.
abstract: Hydrodynamics predicts that swimming bacteria generate a propulsion force when a helical flagellum rotates because rotating helices necessarily translate at a low Reynolds number. It is generally believed that the flagella of motile bacteria are semirigid helices with a fixed pitch determined by hydrodynamic principles. Here, we report the characterization of three mutations in laboratory strains of Escherichia coli that produce different steady-state flagella without losing cell motility. E. coli flagella rotate counterclockwise during forward swimming, and the normal form of the flagella is a left-handed helix. A single amino acid exchange A45G and a double mutation of A48S and S110A change the resting flagella to right-handed helices. The stationary flagella of the triple mutant were often straight or slightly curved at neutral pH. Deprotonation facilitates the helix formation of it. The helical and curved flagella can be transformed to the normal form by torsion upon rotation and thus propel the cell. These mutations arose in the long-term laboratory cultivation. However, flagella are under strong selection pressure as extracellular appendages, and similar transformable flagella would be common in natural environments.
authors.affiliation: Department of Bioorganic Chemistry, Max Planck Institute for Chemical Ecology, Jena, Germany.
authors.forename: Wenjing
authors.initials: W
authors.lastname: Wang
authors.forename: Zhengzeng
authors.initials: Z
authors.lastname: Jiang
authors.forename: Martin
authors.initials: M
authors.lastname: Westermann
authors.forename: Liyan
authors.initials: L
authors.lastname: Ping
mesh_terms: D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics* / Q000502:physiology; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D005407:Flagella / Q000737:chemistry / Q000235:genetics* / Q000502:physiology; D005408:Flagellin; D008124:Locomotion; D008958:Models, Molecular; D020125:Mutation, Missense; D017354:Point Mutation; D011487:Protein Conformation
chemical_list: D029968:Escherichia coli Proteins; C516095:FliC protein, E coli; D005408:Flagellin