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PMID: 12885631 Published · ppublish English Comparative Study Evaluation Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Validation Study

The motility of mollicutes.

Biophysical journal ·Vol. 85 ·No. 2 ·2003-08-00 ·Pages 828-42

Wolgemuth CW, Igoshin O, Oster G

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.

MeSH Terms
Bacterial Physiological Phenomena Computer Simulation Mechanotransduction, Cellular/physiology Models, Biological Models, Chemical Molecular Motor Proteins/chemistry,physiology Motion Mycoplasma/chemistry,physiology Species Specificity Spiroplasma/chemistry,physiology Stress, Mechanical Swimming/physiology Tenericutes/chemistry,physiology
Chemicals
Molecular Motor Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Wolgemuth Charles W
Department of Physiology, University of Connecticut Health Center, Farmington, Connecticut, USA.
Igoshin Oleg
Oster George
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
2003-08-00
Pages
828-42
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1303205
Subset
IM
Grants
NIGMS NIH HHS · R01 GM059875 · United States
NIGMS NIH HHS · GM59875-02 · United States
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