DOI: 10.1128/jb.182.11.3022-3028.2000. Deletion Analysis of the Flagellar Switch Protein FliG of <i>Salmonella</i>

Deletion Analysis of the Flagellar Switch Protein FliG of Salmonella

10.1128/jb.182.11.3022-3028.2000

Crossref journal-article

American Society for Microbiology

Journal of Bacteriology (235)

Abstract

ABSTRACT The flagellar motor/switch complex, consisting of the three proteins FliG, FliM, and FliN, plays a central role in bacterial motility and chemotaxis. We have analyzed FliG, using 10-amino-acid deletions throughout the protein and testing the deletion clones for their motility and dominance properties and for interaction of the deletion proteins with the MS ring protein FliF. Only the N-terminal 46 amino acids of FliG (segments 1 to 4) were important for binding to FliF; consistent with this, an N-terminal fragment consisting of residues 1 to 108 bound FliF strongly, whereas a C-terminal fragment consisting of residues 109 to 331 did not bind FliF at all. Deletions in the region from residues 37 to 96 (segments 4 to 9), 297 to 306 (segment 30), and 317 to 326 (segment 32) permitted swarming, though not at wild-type levels; all other deletions caused paralyzed or, more commonly, nonflagellate phenotype. Except for those near the N terminus, deletions had a dominant negative effect on wild-type cells.

Bibliography

Kihara, M., Miller, G. U., & Macnab, R. M. (2000). Deletion Analysis of the Flagellar Switch Protein FliG of Salmonella. Journal of Bacteriology, 182(11), 3022â3028.

Authors 3

May Kihara (first)
Gabriele U. Miller (additional)
Robert M. Macnab (additional)

References 29 Referenced 51

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Fan F. Ohnishi K. Francis N. R. Macnab R. M. The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal body.Mol. Microbiol.26199710351046 (10.1046/j.1365-2958.1997.6412010.x) / Mol. Microbiol. / The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal body by Fan F. (1997)
Francis N. R. Irikura V. M. Yamaguchi S. DeRosier D. J. Macnab R. M. Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-ring face of the basal body.Proc. Natl. Acad. Sci. USA89199263046308 (10.1073/pnas.89.14.6304) / Proc. Natl. Acad. Sci. USA / Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-ring face of the basal body by Francis N. R. (1992)
Francis N. R. Sosinsky G. E. Thomas D. DeRosier D. J. Isolation, characterization and structure of bacterial flagellar motors containing the switch complex.J. Mol. Biol.235199412611270 (10.1006/jmbi.1994.1079) / J. Mol. Biol. / Isolation, characterization and structure of bacterial flagellar motors containing the switch complex by Francis N. R. (1994)
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Khan I. H. Reese T. S. Khan S. The cytoplasmic component of the bacterial flagellar motor.Proc. Natl. Acad. Sci. USA89199259565960 (10.1073/pnas.89.13.5956) / Proc. Natl. Acad. Sci. USA / The cytoplasmic component of the bacterial flagellar motor by Khan I. H. (1992)
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Dates

Type	When
Created	23 years ago (July 27, 2002, 6 a.m.)
Deposited	4 years ago (July 29, 2021, 1:52 p.m.)
Indexed	1 year, 2 months ago (June 1, 2024, 12:33 a.m.)
Issued	25 years, 2 months ago (June 1, 2000)
Published	25 years, 2 months ago (June 1, 2000)
Published Print	25 years, 2 months ago (June 1, 2000)

Funders 0

None

BibTeX

@article{Kihara_2000, title={Deletion Analysis of the Flagellar Switch Protein FliG of Salmonella}, volume={182}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.182.11.3022-3028.2000}, DOI={10.1128/jb.182.11.3022-3028.2000}, number={11}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Kihara, May and Miller, Gabriele U. and Macnab, Robert M.}, year={2000}, month=jun, pages={3022–3028} }

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