ArticleGenes & development2007
The mechanism of outer membrane penetration by the eubacterial flagellum and implications for spirochete evolution.
Article in Genes & development, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
44 citing papers in PubMed, 68 citations in OpenAlex.
- FlgJ cell-wall hydrolyzing activity enhances, but is not required, for flagellum assembly inJournal of bacteriology · 2026Article
- Active removal of inhibitory components drives the flagellar type 3 secretion-specificity switch.mBio · 2026Article
- Active removal of inhibitory components drives the flagellar Type III Secretion Specificity Switch.bioRxiv : the preprint server for biology · 2026Article
- Evolution of a large periplasmic disk in Campylobacterota flagella enables both efficient motility and autoagglutination.Developmental cell · 2024Article
- Structure and Dynamics of the Bacterial Flagellar Motor Complex.Biomolecules · 2024Review
- FlaG competes with FliS-flagellin complexes for access to FlhA in the flagellar T3SS to controlProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- Modulation of the Enzymatic Activity of the Flagellar Lytic Transglycosylase SltF by Rod Components and the Scaffolding Protein FlgJ inJournal of bacteriology · 2021Article
- Structure of the molecular bushing of the bacterial flagellar motor.Nature communications · 2021Article
- Characterization of the relationship between polar and lateral flagellar genes in clinical Aeromonas dhakensis: phenotypic, genetic and biochemical analyses.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2021Article
- Molecular structure of the intact bacterial flagellar basal body.Nature microbiology · 2021Article
- CwlQ Is Required for Swarming Motility but Not Flagellar Assembly in Bacillus subtilis.Journal of bacteriology · 2021Article
- Architecture and Assembly of the Bacterial Flagellar Motor Complex.Sub-cellular biochemistry · 2021Review
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- Structure of the native supercoiled flagellar hook as a universal joint.Nature communications · 2019Article
- Architecture of the Bacterial Flagellar Distal Rod and Hook ofBiomolecules · 2019Article
- γ-proteobacteria eject their polar flagella under nutrient depletion, retaining flagellar motor relic structures.PLoS biology · 2019Article
- Assembly Order of Flagellar Rod Subunits in Bacillus subtilis.Journal of bacteriology · 2018Article
- The Vibrio H-Ring Facilitates the Outer Membrane Penetration of the Polar Sheathed Flagellum.Journal of bacteriology · 2018Article
- Biochemical and Phylogenetic Study of SltF, a Flagellar Lytic Transglycosylase from Rhodobacter sphaeroides.Journal of bacteriology · 2018Article
Corrections and comments
- Commented on by
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The rod component of the bacterial flagellum polymerizes from the inner membrane across the periplasmic space and stops at a length of 25 nm at the outer membrane. Bushing structures, the P- and L-rings, polymerize around the distal rod and form a pore in the outer membrane. The flagellar hook structure is then added to the distal rod growing outside the cell. Hook polymerization stops after the rod-hook structure reaches approximately 80 nm in length. This study describes mutants in the distal rod protein FlgG that fail to terminate rod growth. The mutant FlgG subunits continue to polymerize close to the length of the normal rod-hook structure of 80 nm. These filamentous rod structures have multiple P-rings and fail to form the L-ring pore at the outer membrane. The flagella grow within the periplasm similar to spirochete flagella. This provides a simple method to evolve intracellular flagella as in spirochetes. The mechanism that couples rod growth termination to the ring assembly and outer membrane penetration exemplifies the importance of stopping points in the construction of a complex macromolecular machine that facilitate efficient coupling to the next step in the assembly pathway.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.