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-Structure paper
Title | Bacterial flagella hijack type IV pili proteins to control motility. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 121, Issue 4, Page e2317452121, Year 2024 |
Publish date | Jan 23, 2024 |
Authors | Xiaolin Liu / Shoichi Tachiyama / Xiaotian Zhou / Rommel A Mathias / Sharmin Q Bonny / Mohammad F Khan / Yue Xin / Anna Roujeinikova / Jun Liu / Karen M Ottemann / |
PubMed Abstract | 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 ...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 links | Proc Natl Acad Sci U S A / PubMed:38236729 / PubMed Central |
Methods | EM (subtomogram averaging) |
Resolution | 31.0 - 39.0 Å |
Structure data | EMDB-40405: In situ structure of Helicobacter pylori flagellar motor. EMDB-40406: In situ structure of Helicobacter pylori flagellar motor from PilN and PilO deletion mutant |
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