amphitrichous

Edge evidence

• bacterial-type flagellum defines amphitrichous METPO:2007500

  Flagella at both cell poles define the amphitrichous arrangement.

  • DOI:10.1093/femsre/fuv034 Schuhmacher et al. describe bipolar (amphitrichous) flagellation governed by FlhF/FlhG.
• amphitrichous associated with bipolar placement biolink:associated_with

  The amphitrichous pattern places flagella at both poles.

  • DOI:10.3390/biom9070279 Flagellum review supports polar flagellar filaments as locomotory organelles.
• FlhF binds FliG

  FlhF specifically interacts with the polar-system FliG to initiate assembly.

  • DOI:10.1038/s41467-024-50274-4 FlhF exhibited a strong interaction with FliG and specifically interacts with FliG from the polar flagellar system.
• FliG binds FliF (MS-ring)

  FlhF-bound FliG captures FliF, promoting MS-ring formation at the pole.

  • DOI:10.1038/s41467-024-50274-4 When bound to FlhF, FliG was able to interact with the cytoplasmic domain of the MS-ring forming protein FliF.
• FlhF localizes to cell pole biolink:located_in

  GTP-bound dimeric FlhF localizes to the cell pole to nucleate flagellar assembly.

  • DOI:10.7554/eLife.93004.3 GTP-bound dimeric FlhF localizes to the cell pole where it recruits the initial flagellar building blocks.
• FipA directly interacts with FlhF

  FipA directly interacts with FlhF and facilitates its polar recruitment.

  • DOI:10.7554/eLife.93004.3 In all three species, FipA directly interacts with FlhF and facilitates its recruitment to the membrane at the cell pole.
• FipA promotes FlhF polar localization RO:0002213

  Loss of FipA significantly decreases polar localization of FlhF.

  • DOI:10.7554/eLife.93004.3 In the absence of FipA, polar localization of FlhF was significantly decreased in all three species.
• FlhG stimulates GTPase activity of FlhF

  ATP-bound FlhG dimer stimulates FlhF GTPase activity, controlling its polar dynamics.

  • DOI:10.7554/eLife.93004.3 The ATP-bound FlhG dimer can interact with the GTP-bound FlhF dimer, thereby stimulating its GTPase activity.
• FlhG restricts polar flagellar number

  FlhG links flagella synthesis with transcription and restricts polar flagellar number.

  • DOI:10.7554/eLife.93004.3 FlhG links flagella synthesis with transcription regulation and effectively restricts the number of polar flagella that are formed.