title: The motility of mollicutes.
abstract: Recent experiments show that the conformation of filament proteins play a role in the motility and morphology of many different types of bacteria. Conformational changes in the protein subunits may produce forces to drive propulsion and cell division. Here we present a molecular mechanism by which these forces can drive cell motion. Coupling of a biochemical cycle, such as ATP hydrolysis, to the dynamics of elastic filaments enable elastic filaments to propagate deformations that generate propulsive forces. We demonstrate this possibility for two classes of wall-less bacteria called mollicutes: the swimming of helical-shaped Spiroplasma, and the gliding motility of Mycoplasma.
authors.affiliation: Department of Physiology, University of Connecticut Health Center, Farmington, Connecticut, USA.
authors.forename: Charles W
authors.initials: CW
authors.lastname: Wolgemuth
authors.forename: Oleg
authors.initials: O
authors.lastname: Igoshin
authors.forename: George
authors.initials: G
authors.lastname: Oster
mesh_terms: D018407:Bacterial Physiological Phenomena; D003198:Computer Simulation; D040542:Mechanotransduction, Cellular / Q000502:physiology*; D008954:Models, Biological; D008956:Models, Chemical; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000502:physiology*; D009038:Motion; D009174:Mycoplasma / Q000737:chemistry / Q000502:physiology; D013045:Species Specificity; D013149:Spiroplasma / Q000737:chemistry / Q000502:physiology; D013314:Stress, Mechanical; D013550:Swimming / Q000502:physiology; D008973:Tenericutes / Q000737:chemistry* / Q000502:physiology*
chemical_list: D020409:Molecular Motor Proteins