Many bacteria swim in liquids and move over solid surfaces by rotating flagella. The bacterial flagellum is a supramolecular protein complex that is composed of about 30 different flagellar proteins ranging from a few to tens of thousands. Despite structural and functional diversities of the flagella among motile bacteria, the flagellum commonly consists of a membrane-embedded rotary motor fueled by an ion motive force across the cytoplasmic membrane, a universal joint, and a helical propeller that extends several micrometers beyond the cell surface. The flagellar motor consists of a rotor and several stator units, each of which acts as a transmembrane ion channel complex that converts the ion flux through the channel into the mechanical work required for force generation. The rotor ring complex is equipped with a reversible gear that is regulated by chemotactic signal transduction pathways. As a result, bacteria can move to more desirable locations in response to environmental changes. Recent high-resolution structural analyses of flagella using cryo-electron microscopy have provided deep insights into the assembly, rotation, and directional switching mechanisms of the flagellar motor complex. In this review article, we describe the current understanding of the structure and dynamics of the bacterial flagellum.
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http://dx.doi.org/10.3390/biom14121488 | DOI Listing |
Int J Food Microbiol
January 2025
College of Food Science and Engineering, Northwest A&F University, Yangling, Shaanxi 712100, China. Electronic address:
Proc Natl Acad Sci U S A
January 2025
Chinese Academy of Sciences Key Laboratory of Tropical Marine Bio Resources and Ecology, Guangdong Key Laboratory of Marine Materia Medica, Innovation Academy of South China Sea Ecology and Environmental Engineering, Guangdong Provincial Observation and Research Station for Coastal Upwelling Ecosystem, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou 511458, China.
Rotation of the bacterial flagellum, the first identified biological rotary machine, is driven by its stator units. Knowledge gained about the function of stator units has increasingly led to studies of rotary complexes in different cellular pathways. Here, we report that a tetrameric PilZ family protein, FlgX, is a structural component underneath the stator units in the flagellar motor of .
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
Department of Macromolecular Science, Graduate School of Science, Osaka University, Toyonaka 560-0043, Japan.
Many bacteria swim in liquid or swarm on surface using the flagellum rotated by a motor driven by specific ion flow. The motor consists of the rotor and stator, and the stator converts the energy of ion flow to mechanical rotation. However, the ion pathway and the mechanism of stator rotation coupled with specific ion flow are still obscure.
View Article and Find Full Text PDFPLoS Pathog
January 2025
Department of Microbiology, University of Georgia, Athens, Georgia, United States of America.
The Helicobacter pylori flagellar motor contains several accessory structures that are not found in the archetypal Escherichia coli and Salmonella enterica motors. H. pylori hp0838 encodes a previously uncharacterized lipoprotein and is in an operon with flgP, which encodes a motor accessory protein.
View Article and Find Full Text PDFPLoS Pathog
January 2025
Microbial Sciences Institute, Yale University, West Haven, Connecticut, United States of America.
Spirochetes are a widespread group of bacteria with a distinct morphology. Some spirochetes are important human pathogens that utilize periplasmic flagella to achieve motility and host infection. The motors that drive the rotation of periplasmic flagella have a unique spirochete-specific feature, termed the collar, crucial for the flat-wave morphology and motility of the Lyme disease spirochete Borrelia burgdorferi.
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