ArticlePloS one2015
Weak Interactions between Salmonella enterica FlhB and Other Flagellar Export Apparatus Proteins Govern Type III Secretion Dynamics.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Article
- A real-time assay for cell-penetrating peptide-mediated delivery of molecular cargos.PloS one · 2021Article
- The flexible linker of the secreted FliK ruler is required for export switching of the flagellar protein export apparatus.Scientific reports · 2020Article
- FliK-Driven Conformational Rearrangements of FlhA and FlhB Are Required for Export Switching of the Flagellar Protein Export Apparatus.Journal of bacteriology · 2020Article
- Flagellar Basal Body Structural Proteins FlhB, FliM, and FliY Are Required for Flagellar-Associated Protein Expression inFrontiers in microbiology · 2018Article
- Assembly and stoichiometry of the core structure of the bacterial flagellar type III export gate complex.PLoS biology · 2017Article
- A versatile cell-penetrating peptide-adaptor system for efficient delivery of molecular cargos to subcellular destinations.PloS one · 2017Article
- Novel cell-penetrating peptide-adaptors effect intracellular delivery and endosomal escape of protein cargos.Journal of cell science · 2016Article
- The Structure of a Type 3 Secretion System (T3SS) Ruler Protein Suggests a Molecular Mechanism for Needle Length Sensing.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The bacterial flagellum contains its own type III secretion apparatus that coordinates protein export with assembly at the distal end. While many interactions among export apparatus proteins have been reported, few have been examined with respect to the differential affinities and dynamic relationships that must govern the mechanism of export. FlhB, an integral membrane protein, plays critical roles in both export and the substrate specificity switching that occurs upon hook completion. Reported herein is the quantitative characterization of interactions between the cytoplasmic domain of FlhB (FlhBC) and other export apparatus proteins including FliK, FlhAC and FliI. FliK and FlhAC bound with micromolar affinity. KD for FliI binding in the absence of ATP was 84 nM. ATP-induced oligomerization of FliI induced kinetic changes, stimulating fast-on, fast-off binding and lowering affinity. Full length FlhB purified under solubilizing, nondenaturing conditions formed a stable dimer via its transmembrane domain and stably bound FliH. Together, the present results support the previously hypothesized central role of FlhB and elucidate the dynamics of protein-protein interactions in type III secretion.
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