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TitleBacterial flagella hijack type IV pili proteins to control motility.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 121, Issue 4, Page e2317452121, Year 2024
Publish dateJan 23, 2024
AuthorsXiaolin Liu / Shoichi Tachiyama / Xiaotian Zhou / Rommel A Mathias / Sharmin Q Bonny / Mohammad F Khan / Yue Xin / Anna Roujeinikova / Jun Liu / Karen M Ottemann /
PubMed AbstractBacterial flagella and type IV pili (TFP) are surface appendages that enable motility and mechanosensing through distinct mechanisms. These structures were previously thought to have no components in ...Bacterial flagella and type IV pili (TFP) are surface appendages that enable motility and mechanosensing through distinct mechanisms. These structures were previously thought to have no components in common. Here, we report that TFP and some flagella share proteins PilO, PilN, and PilM, which we identified as part of the flagellar motor. mutants lacking PilO or PilN migrated better than wild type in semisolid agar because they continued swimming rather than aggregated into microcolonies, mimicking the TFP-regulated surface response. Like their TFP homologs, flagellar PilO/PilN heterodimers formed a peripheral cage that encircled the flagellar motor. These results indicate that PilO and PilN act similarly in flagella and TFP by differentially regulating motility and microcolony formation when bacteria encounter surfaces.
External linksProc Natl Acad Sci U S A / PubMed:38236729 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution31.0 - 39.0 Å
Structure data

EMDB-40405: In situ structure of Helicobacter pylori flagellar motor.
Method: EM (subtomogram averaging) / Resolution: 31.0 Å

EMDB-40406: In situ structure of Helicobacter pylori flagellar motor from PilN and PilO deletion mutant
Method: EM (subtomogram averaging) / Resolution: 39.0 Å

Source
  • Helicobacter pylori G27 (bacteria)

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