monotrichous

Edge evidence

• bacterial-type flagellum defines monotrichous METPO:2007500

  A single polar flagellum defines the monotrichous arrangement.

  • DOI:10.1093/femsre/fuv034 Schuhmacher et al. describe single-flagellum (monotrichous) polar flagellation.
• monotrichous associated with polar single-flagellum placement biolink:associated_with

  The monotrichous pattern places one flagellum at one pole.

  • DOI:10.3390/biom9070279 Flagellum review supports a single helical flagellar filament as a locomotory organelle.
• FlhF promotes localization of polar localization of flagellum

  FlhF promotes targeting of flagella to the cell pole; deleting flhF causes mislocalization to nonpolar sites.

  • DOI:10.1128/jb.00110-23 FlhF and FlhG control the location and number of flagella in many polar-flagellated bacteria; deleting flhF caused hypoflagellation and mislocalization of flagella to nonpolar sites.
• FlhG regulates number of flagellum number per cell

  FlhG regulates the number of flagella per cell; its loss in single-flagellum bacteria often causes hyperflagellation.

  • DOI:10.1128/jb.00110-23 FlhF and FlhG control the location and number of flagella respectively; deleting flhG in bacteria with a single polar flagellum often results in hyperflagellation.
• FlhF binds FliG

  The FlhF B-domain FliG-Interaction Domain (FID) binds FliG.

  • DOI:10.1038/s41467-024-50274-4 The FlhF B-domain contains an N-terminal FliG Interaction Domain (FID); the N-terminal ~60 aa of the B-domain are necessary and sufficient for FliG binding.
• FliG recruits FliF MS-ring protein

  FlhF-bound FliG engages the MS-ring protein FliF, recruiting a FliF-FliG complex to the pole.

  • DOI:10.1038/s41467-024-50274-4 FlhF-bound FliG then engages the MS-ring protein FliF, effectively recruiting a FliF-FliG complex to the pole.
• FlhF hinders interaction of FliM/FliN C-ring partners

  FlhF-bound FliG can still engage FliF but is prevented from interacting with C-ring partners FliM/FliN.

  • DOI:10.1038/s41467-024-50274-4 FlhF-bound FliG can still engage the cytoplasmic domain of FliF but is prevented from interacting with C-ring partners FliM/FliN.
• FlhG stimulates GTPase activity of FlhF

  FlhG stimulates FlhF GTPase activity, modulating FlhF control over FliG interactions.

  • DOI:10.1038/s41467-024-50274-4 FlhG's modulation of FlhF controls FliG's interaction with FliM/FliN; FlhG stimulates FlhF GTPase activity.