ArticleJournal of bacteriology2014
The flagellar soluble protein FliK determines the minimal length of the hook in Salmonella enterica serovar Typhimurium.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- 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
- The flexible linker of the secreted FliK ruler is required for export switching of the flagellar protein export apparatus.Scientific reports · 2020Article
- Beyond a Ribosomal RNA Methyltransferase, the Wider Role of MraW in DNA Methylation, Motility and Colonization inFrontiers in microbiology · 2019Article
- Nanoscale-length control of the flagellar driveshaft requires hitting the tethered outer membrane.Science (New York, N.Y.) · 2017Article
- Genetic and Transcriptional Analyses of the Flagellar Gene Cluster in Actinoplanes missouriensis.Journal of bacteriology · 2016Article
- Identification of the Key Sequence in the FliK C-Terminal Domain for Substrate Specificity Switching in the Flagellar Protein Secretion.Journal of bacteriology · 2016Article
- Structural Characterization of the Fla2 Flagellum of Rhodobacter sphaeroides.Journal of bacteriology · 2015Article
- Differential single nucleotide polymorphism-based analysis of an outbreak caused by Salmonella enterica serovar Manhattan reveals epidemiological details missed by standard pulsed-field gel electrophoresis.Journal of clinical microbiology · 2015Article
- Weak Interactions between Salmonella enterica FlhB and Other Flagellar Export Apparatus Proteins Govern Type III Secretion Dynamics.PloS one · 2015Article
- Comparative analysis of the secretion capability of early and late flagellar type III secretion substrates.Molecular microbiology · 2014Article
- Analysis of factors that affect FlgM-dependent type III secretion for protein purification with Salmonella enterica serovar Typhimurium.Journal of bacteriology · 2014Article
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2 authors.
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Abstract
The length of the flagellar hook is controlled by the soluble protein FliK. FliK is structurally divided into two halves with distinct functions; the N-terminal half determines hook length, while the C-terminal half switches the secretion substrate specificity, consequently terminating hook elongation. FliK properly achieves both functions only when it is secreted. In a previous paper, we showed that a temperature-sensitive flgE mutant of Salmonella enterica serovar Typhimurium, SJW2219, produced basal bodies with short hooks (average length, 25 nm) at 37°C. In this study, we show that the mutant cells grown at 37°C secrete FliK but not flagellin (FliC), indicating that FliK is abortively secreted into the medium when the hook is shorter than 30 nm. In contrast, FliK unfailingly switches the gate modes when the hook is longer than 30 nm. Taking the FliC, FliK, and FlgM secretion patterns into account, we conclude that FliK determines the minimal length of the hook. We will discuss how FliK detects the critical switching point of the secretion gate.
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