Role of gene flaFV on flagellar hook formation in Salmonella typhimurium

Kutsukake, Kazuhiro; Suzuki, Takayuki; Yamaguchi, Shigeru; Iino, Tetsuo

doi:10.1128/jb.140.1.267-275.1979

Cited by 37 publications

(13 citation statements)

References 34 publications

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“…The formation of hooks follows the completion of flagellar basal bodies and precedes the growth of flagellar filaments at their distal tips. The structural gene for the hook monomer has been identified as flaFV (18). Several cistrons other than flaFV are required for the formation of flagellar filaments at the tips of hooks.…”

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confidence: 99%

Role of the flaR gene in flagellar hook formation in Salmonella spp

Suzuki¹,

Iino²

1981

J Bacteriol

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Flagellar filaments were reconstituted by polymerization with exogenously supplied flagellin monomers at the tips of normal hooks on Salmonella cells which were missing the filaments because of mutations in either the flaL or flaU gene or the flagellin genes H1 and H2. Reconstitution did not occur at the tips of polyhooks of the flaR mutant cells. Thus, the absence of flagellar filaments in the flaR mutant cells was probably caused by the inability of the polyhooks to work as polymerization nuclei for flagellin. A Phf+ mutant which produced polyhooks with flagellar filaments was isolated from a flaR polyhook mutant. Genetic analysis of the Phf+ mutant showed that it carried an intracistronic suppressor mutation of the original flaR mutation. This result indicated that the flaR gene regulates hook length and initiates flagellin formation.

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confidence: 99%

Role of the flaR gene in flagellar hook formation in Salmonella spp

Suzuki¹,

Iino²

1981

J Bacteriol

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“…It is interesting to see that our hook shape mutant resembles some of the hook shape mutants previously isolated by Kutsukake et al (1979), although the isolation procedures were quite different (see Discussion).…”

Section: Dna Sequencing Of the Suppressor In Sjw3122mentioning

confidence: 76%

“…The SJW3122 strain adds another example to the hook shape mutants reported previously by Kutsukake et al (1979). The isolation procedures of mutants from the two groups were quite different.…”

Section: Discussionmentioning

confidence: 99%

Flagellar filament elongation can be impaired by mutations in the hook protein FlgE of Salmonella typhimurium: a possible role of the hook as a passage for the anti‐sigma factor FlgM

Saitō

Ueno

Kubori

et al. 1998

Molecular Microbiology

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SummaryAmong motile revertants isolated from flagellar hookdeficient (flgE ) mutants of Salmonella typhimurium, one produced only short flagellar filaments in L broth, despite the fact that flagellin itself has the ability to polymerize into long filaments in vitro. This pseudorevertant has an intragenic suppressor, resulting in a two-amino-acid substitution (Asp-Gln→Ala-Arg) in the C-terminal region of the hook protein, FlgE. The flagellation of the pseudorevertant was greatly affected by the concentration of NaCl in the culture media: we observed no filaments in the absence of NaCl, short filaments in 1% NaCl and full-length filaments in 2% NaCl. Electron microscopy of osmotically shocked cells showed that the number of hook-basal bodies on cells was constant under various NaCl conditions. Furthermore, we found that the mutant hook was straight rather than curved. We monitored the cellular flagellin level of this pseudorevertant under various NaCl concentrations by immunoblotting. It was revealed that little flagellin was present under NaCl-free conditions in contrast with the ordinary amounts of flagellin present in 2% NaCl. As the expression of flagellin is regulated by competitive interaction of a sigma factor, FliA, and a corresponding anti-sigma factor, FlgM, we also observed the effect of NaCl on the secretion of FlgM. FlgM was secreted into the media in more than 1% NaCl but accumulated inside the cells in the absence of NaCl, indicating that the failure of secretion of FlgM in the absence of salt was the cause of the impaired elongation of filaments.

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“…However, the flagellum in these FlaTs mutants is fully functional at the permissive temperature, and it is difficult to imagine a defective modification that would permit function at the permissive temperature yet prevent it at the restrictive temperature. The direct conclusion that the altered protein is the product of the mutated gene is certainly valid forflaFV, whose product is the 42K hook protein (27,31). We regard this as a vindication of our interpretation of the results for the other genes.…”

Section: Vol 161 1985mentioning

confidence: 84%

Purification and characterization of the flagellar hook-basal body complex of Salmonella typhimurium

Aizawa¹,

Dean²,

Jones³

et al. 1985

J Bacteriol

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The hook-basal body complex of Salmonella typhimurium, a major component of its flageUar apparatus, was subjected to detailed analysis by electron microscopy and gel electrophoresis. The study was facilitated by the development of an improved protocol for isolation of the complexes in high yield and purity. Nine proteins were identified with the structure. These proteins had apparent molecular weights of 65,and 14K. Small but reproducible shifts in the apparent molecular weights of specific proteins from conditionally nonflagellate mutants indicated the following gene-polypeptide correspondences: flaFV, 42K; flaFVI, 32K; flaFVII, 30K; J IaFIX, 38K; flaAII.I, 65K. Several new morphological features of hook-basal body complexes were recognized, including a clawlike structure on the cytoplasm-proximal M ring and additionai material at the cytoplasmic face of the M ring. Based on this study and the work ot others, we suggest that the morphological features of the hook-basal body complex correspond to the following proteins: hook-filament junction, 60K; hook, 42K; rod, 30K and 32K; L ring and outer cylinder wall, 27K; P ring, 38K; S ring,-unknown; M ring, 65K.

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Role of gene flaFV on flagellar hook formation in Salmonella typhimurium

Cited by 37 publications

References 34 publications

Role of the flaR gene in flagellar hook formation in Salmonella spp

Role of the flaR gene in flagellar hook formation in Salmonella spp

Flagellar filament elongation can be impaired by mutations in the hook protein FlgE of Salmonella typhimurium: a possible role of the hook as a passage for the anti‐sigma factor FlgM

Purification and characterization of the flagellar hook-basal body complex of Salmonella typhimurium

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