Structure of the molecular bushing of the bacterial flagellar motor

Yamaguchi, Tomoko; Makino, Fumiaki; Miyata, Tomoko; Minamino, Tetsuo; Kato, Takayuki; Namba, Keiichi

doi:10.1038/s41467-021-24715-3

Cited by 41 publications

(29 citation statements)

References 55 publications

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“…Replacing this with a positively charged lysine residue would alter the electrostatic potential in this area, potentially interfering with phage assembly. It is therefore likely that a mixture of both attractive and repulsive forces are important for phage assembly and egress, similar to the findings reported for the assembly and rotation of the bacterial flagellar rod 49 .…”

Section: Discussionsupporting

confidence: 80%

CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage

Conners

McLaren

Łapińska

et al. 2021

Preprint

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The Ff family of filamentous bacteriophages infect gram-negative bacteria, but do not cause lysis of their host cell. Instead, new virions are extruded via the phage-encoded pIV protein, which has homology with bacterial secretins. Here, we have determined the structure of pIV from the f1 filamentous bacteriophage at 2.7 A resolution by cryo-electron microscopy, the first near-atomic structure of a phage secretin. Fifteen f1 pIV monomers assemble to form a gated channel in the bacterial outer membrane, with associated soluble domains projecting into the periplasm. We model channel opening and propose a mechanism for phage-mediated gate movement. By single-cell microfluidics experiments, we demonstrate the potential for secretins such as pIV to be used as adjuvants to increase the uptake and efficacy of antibiotics in bacteria. Finally, we compare the f1 pIV structure to its homologues to reveal similarities and differences between phage and bacterial secretins.

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Section: Discussionsupporting

confidence: 80%

CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage

Conners

McLaren

Łapińska

et al. 2021

Preprint

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“…Recently, Johnson et al (2021), Yamaguchi et al (2021), and Tan et al (2021) reported the molecular structures of the flagellar P‐ and L‐rings from S. enterica . Johnson and colleagues observed an outer ring formed by a protein called YecR surrounding the L‐ring in their structure, which they hypothesized helps to remodel the lipid bilayer around the L‐ring protein, thereby facilitating its assembly in the OM.…”

Section: Discussionmentioning

confidence: 99%

Novel transient cytoplasmic rings stabilize assembling bacterial flagellar motors

et al. 2022

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The process by which bacterial cells build their intricate flagellar motility apparatuses has long fascinated scientists. Our understanding of this process comes mainly from studies of purified flagella from two species, Escherichia coli and Salmonella enterica.Here, we used electron cryo-tomography (cryo-ET) to image the assembly of the flagellar motor in situ in diverse Proteobacteria: Hylemonella gracilis, Helicobacter pylori, Campylobacter jejuni, Pseudomonas aeruginosa, Pseudomonas fluorescens, and Shewanella oneidensis. Our results reveal the in situ structures of flagellar intermediates, beginning with the earliest flagellar type III secretion system core complex (fT3SScc) and MS-ring. In high-torque motors of Beta-, Gamma-, and Epsilon-proteobacteria, we discovered novel cytoplasmic rings that interact with the cytoplasmic torque ring formed by FliG. These rings, associated with the MSring, assemble very early and persist until the stators are recruited into their periplasmic ring; in their absence the stator ring does not assemble. By imaging mutants in Helicobacter pylori, we found that the fT3SScc proteins FliO and FliQ are required for the assembly of these novel cytoplasmic rings. Our results show that rather than a simple accretion of components, flagellar motor assembly is a dynamic process in which accessory components interact transiently to assist in building the complex nanomachine.

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“…Like GldK/PorK, FlgH is a lipoprotein and like GldN/PorN, FlgI is a periplasmic protein. The LP ring of the flagellar motor interacts with the distal end of the driveshaft (rod), supports stable rotation of the rod, and reduces friction ( Yamaguchi et al, 2021 ). The GldK/PorK-N ring may play a similar role in T9SS rotation.…”

Section: The Mechanism Of Rotation and Comparison Of Type 9 Secretion...mentioning

confidence: 99%

Design Principles of the Rotary Type 9 Secretion System

et al. 2022

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The Fo ATP synthase, the bacterial flagellar motor, and the bacterial type 9 secretion system (T9SS) are the three known proton motive force driven biological rotary motors. In this review, we summarize the current information on the nuts and bolts of T9SS. Torque generation by T9SS, its role in gliding motility of bacteria, and the mechanism via which a T9SS-driven swarm shapes the microbiota are discussed. The knowledge gaps in our current understanding of the T9SS machinery are outlined.

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Structure of the molecular bushing of the bacterial flagellar motor

Cited by 41 publications

References 55 publications

CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage

CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage

Novel transient cytoplasmic rings stabilize assembling bacterial flagellar motors

Design Principles of the Rotary Type 9 Secretion System

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