In situ structure of the <i>Caulobacter crescentus</i> flagellar motor and visualization of binding of a CheY‐homolog

Roßmann, Florian; Hug, Isabelle; Sangermani, Matteo; Jenal, Urs; Beeby, Morgan

doi:10.1111/mmi.14525

Cited by 21 publications

(15 citation statements)

References 63 publications

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“…Second, density similar in location and shape has been shown two recent studies to be CheY-P. Chang et al have used GFP-tagged CheY-P to show that, in Borrelia burgdorferi , CheY-P occupies the same position ( Chang et al, 2020 ). Rossmann et al also identified similar density for the CheY homolog, CleD in Caulobacter crescentus ( Rossmann et al, 2020 ). Third, when we place the crystal structure of CheY into the model, there is about 60 Å gap between the C-ring density and this additional density ( Figure 3—figure supplement 2 ).…”

Section: Resultsmentioning

confidence: 83%

The flagellar motor of Vibrio alginolyticus undergoes major structural remodeling during rotational switching

Carroll

Nishikino

Guo

et al. 2020

eLife

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The bacterial flagellar motor switches rotational directions between counterclockwise (CCW) and clockwise (CW) to direct the migration of the cell. The cytoplasmic ring (C-ring) of the motor, which is composed of FliG, FliM, and FliN, is known for controlling the rotational sense of the flagellum. However, the mechanism underlying rotational switching remains elusive. Here, we deployed cryo-electron tomography to visualize the C-ring in two rotational biased mutants in Vibrio alginolyticus. We determined the C-ring molecular architectures, providing novel insights into the mechanism of rotational switching. We report that the C-ring maintained 34-fold symmetry in both rotational senses and the protein composition remained constant. The two structures show FliG conformational changes elicit a large conformational rearrangement of the rotor complex that coincides with rotational switching of the flagellum. FliM and FliN form a stable spiral-shaped base of the C-ring, likely stabilizing the C-ring during the conformational remodeling.

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Section: Resultsmentioning

confidence: 83%

The flagellar motor of Vibrio alginolyticus undergoes major structural remodeling during rotational switching

Carroll

Nishikino

Guo

et al. 2020

eLife

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“…It was recently shown that the chemotaxis response regulator CheY interacts with the C‐ring of fully assembled flagella, forming an associated ring ~ 50 nm in diameter that locks the switch complex in clockwise direction by interacting with the C‐ring protein FliM (Carroll et al , 2020; Chang et al , 2020; Rossmann et al , 2020). While superficially similar, the novel rings we discovered assemble before FliM and even in its absence (in ∆ fliM fliP* H. pylori ), indicating that they are of a different nature.…”

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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“…By performing subtomogram averaging on the identified PL-subcomplexes, we found that they contain, in addition to the P-and L-rings, two other periplasmic rings known as the outer membrane (OM) ring and the cogwheel (Fig. 1J), which are also present in the fully-assembled motor of C. crescentus 12 . These two rings were not visible in the PL-subcomplex previously reported on the poles of swarmer cells due to the low number of particles identified at the time 3 .…”

mentioning

confidence: 99%

Programmed Flagellar Ejection in Caulobacter crescentus Leaves PL-subcomplexes

Kaplan

Wang

Chreifi

et al. 2021

Journal of Molecular Biology

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This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

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In situ structure of the Caulobacter crescentus flagellar motor and visualization of binding of a CheY‐homolog

Cited by 21 publications

References 63 publications

The flagellar motor of Vibrio alginolyticus undergoes major structural remodeling during rotational switching

The flagellar motor of Vibrio alginolyticus undergoes major structural remodeling during rotational switching

Novel transient cytoplasmic rings stabilize assembling bacterial flagellar motors

Programmed Flagellar Ejection in Caulobacter crescentus Leaves PL-subcomplexes

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