ArticleJournal of bacteriology1999
Effect of hook subunit concentration on assembly and control of length of the flagellar hook of Salmonella.
Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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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
16 citing papers in PubMed, 39 citations in OpenAlex.
- Proteome and Physiological Characterization of Halotolerant Nodule Endophytes: The Case ofMicroorganisms · 2022Article
- A tetratricopeptide repeat domain protein has profound effects on assembly of periplasmic flagella, morphology and motility of the lyme disease spirochete Borrelia burgdorferi.Molecular microbiology · 2018Article
- Molecular ruler determines needle length for the Salmonella Spi-1 injectisome.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Mystery of fliK in length control of the flagellar hook.Journal of bacteriology · 2012Article
- Helicobacter pylori exploits a unique repertoire of type IV secretion system components for pilus assembly at the bacteria-host cell interface.PLoS pathogens · 2011Article
- An infrequent molecular ruler controls flagellar hook length in Salmonella enterica.The EMBO journal · 2011Article
- The role of the FliK molecular ruler in hook-length control in Salmonella enterica.Molecular microbiology · 2010Article
- Coordinating assembly of a bacterial macromolecular machine.Nature reviews. Microbiology · 2008Review
- The FliK protein and flagellar hook-length control.Protein science : a publication of the Protein Society · 2007Review
- The flagellar-specific transcription factor, sigma28, is the Type III secretion chaperone for the flagellar-specific anti-sigma28 factor FlgM.Genes & development · 2006Article
- MotD of Sinorhizobium meliloti and related alpha-proteobacteria is the flagellar-hook-length regulator and therefore reassigned as FliK.Journal of bacteriology · 2006Article
- Spa32 regulates a switch in substrate specificity of the type III secreton of Shigella flexneri from needle components to Ipa proteins.Journal of bacteriology · 2002Article
- Shigella Spa32 is an essential secretory protein for functional type III secretion machinery and uniformity of its needle length.Journal of bacteriology · 2002Article
- Relationship between genotype and phenotype of flagellin C in Salmonella.World journal of gastroenterology · 2001Article
- Intergenic suppression between the flagellar MS ring protein FliF of Salmonella and FlhA, a membrane component of its export apparatus.Journal of bacteriology · 2001Article
- Role of FliJ in flagellar protein export in Salmonella.Journal of bacteriology · 2000Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The flagellar hook of Salmonella is a filamentous polymer made up of subunits of the protein FlgE. Hook assembly is terminated when the length reaches about 55 nm. After our recent study of the effect of cellular levels of the hook length control protein FliK, we have now analyzed the effect of cellular levels of FlgE itself. When FlgE was overproduced in a wild-type strain, a fliC (flagellin) mutant, or a fliD (hook-associated protein 2 [HAP2], filament capping protein) mutant, the hooks remained at the wild-type length. In a fliK (hook length control protein) mutant, which produces long hooks (polyhooks), the overproduction of FlgE resulted in extraordinarily long hooks (superpolyhooks). In a flgK (HAP1, first hook-filament junction protein) mutant or a flgL (HAP3, second hook-filament junction protein) mutant, the overproduction of FlgE also resulted in longer than normal hooks. Thus, at elevated hook protein levels not only FliK but also FlgK and FlgL are necessary for the proper termination of hook elongation. When FlgE was severely underproduced, basal bodies without hooks were often observed. However, those hooks that were seen were of wild-type length, demonstrating that FlgE underproduction decreases the probability of the initiation of hook assembly but not the extent of hook elongation.
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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.