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TitleNovel transient cytoplasmic rings stabilize assembling bacterial flagellar motors.
Journal, issue, pagesEMBO J, Vol. 41, Issue 10, Page e109523, Year 2022
Publish dateMay 16, 2022
AuthorsMohammed Kaplan / Catherine M Oikonomou / Cecily R Wood / Georges Chreifi / Poorna Subramanian / Davi R Ortega / Yi-Wei Chang / Morgan Beeby / Carrie L Shaffer / Grant J Jensen /
PubMed AbstractThe 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 ...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 MS-ring, 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.
External linksEMBO J / PubMed:35301732 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution60.0 - 74.0 Å
Structure data

EMDB-25702: Flagellar motor of Hylemonella gracilis
Method: EM (subtomogram averaging) / Resolution: 74.0 Å

EMDB-25703: Flagellar MS-complex of Helicobacter pylori delta fliM fliP*
Method: EM (subtomogram averaging) / Resolution: 66.0 Å

EMDB-25704: Flagellar MS-complex of Helicobacter pylori fliP*
Method: EM (subtomogram averaging) / Resolution: 60.0 Å

EMDB-25705: Flagellar MS-complex of Helicobacter pylori delta fliQ fliP*
Method: EM (subtomogram averaging) / Resolution: 74.0 Å

Source
  • Hylemonella gracilis ATCC 19624 (bacteria)
  • Helicobacter pylori 26695 (bacteria)

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