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TitleCryo-electron Tomography Reveals the Roles of FliY in Flagellar Motor Assembly.
Journal, issue, pagesmSphere, Vol. 7, Issue 1, Page e0094421, Year 2022
Publish dateFeb 23, 2022
AuthorsPing Lu / Huawei Zhang / Yuanzhu Gao / Xudong Jia / Zhe Liu / Daping Wang / Shannon Wing Ngor Au / Qinfen Zhang /
PubMed AbstractHelicobacter pylori plays a causative role in gastric diseases. The pathogenicity of H. pylori depends on its ability to colonize the stomach guided by motility. FliY is a unique flagellar motor ...Helicobacter pylori plays a causative role in gastric diseases. The pathogenicity of H. pylori depends on its ability to colonize the stomach guided by motility. FliY is a unique flagellar motor switch component coexisting with the classical FliG, FliM, and FliN switch proteins in some bacteria and has been shown to be essential for flagellation. However, the functional importance of FliY in H. pylori flagellar motor assembly is not well understood. Here, we applied cryo-electron tomography and subtomogram averaging to analyze the structures of flagellar motors from wild-type strain, -null mutant and complementation mutants expressing the N-terminal or C-terminal domain of FliY. Loss of full-length FliY or its C-terminal domain interrupted the formation of an intact C ring and soluble export apparatus, as well as the hook and flagellar filaments. Complementation with FliY C-terminal domain restored all these missing components of flagellar motor. Taken together, these results provide structural insights into the roles of FliY, especially its C-terminal domain in flagellar motor assembly in H. pylori. Helicobacter pylori is the major risk factor related with gastric diseases. Flagellar motor is one of the most important virulence factors in H. pylori. However, the assembly mechanism of H. pylori flagellar motor is not fully understood yet. Previous report mainly described the overall structures of flagellum but had not focused on its specific components. Here, we focus on H. pylori flagellar C-ring protein FliY. We directly visualize the flagellar structures of H. pylori wild-type and FliY N-/C-terminal complementary strains by cryo-electron tomography and subtomogram averaging. Our results show that deletion of FliY or its C-terminal domain causes the loss of C ring, whereas deletion of FliY N-terminal does not affect C-ring assembly and flagellar structures. Our results provide direct evidence that C-ring protein FliY, especially its C-terminal domain, plays an indispensable role in H. pylori motor assembly and flagellar formation. This study will deepen our understanding about H. pylori pathogenesis.
External linksmSphere / PubMed:35107334 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution55.0 - 73.0 Å
Structure data

EMDB-32908:
Flagellar motor from wild type H. pylori
Method: EM (subtomogram averaging) / Resolution: 65.0 Å

EMDB-32909:
Flagellar motor of H.pylori delta-FliY mutant
Method: EM (subtomogram averaging) / Resolution: 73.0 Å

EMDB-32910:
Flagellar motor of H.pylori FliYc mutant
Method: EM (subtomogram averaging) / Resolution: 55.0 Å

Source
  • Helicobacter pylori (bacteria)

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