Substrate specificity switching of the flagellum-specific export apparatus during flagellar morphogenesis in salmonella typhimurium

Bioscience, Biotechnology and Biochemistry

Volumn 63, Issue 7, 1999, Pages 1301-1303

  Minamino, Tohru ^a,b   Doi, Hiroyuki ^a,c   Kutsukake, Kazuhiro ^a  

^a HIROSHIMA UNIVERSITY   (Japan)

^b YALE UNIVERSITY   (United States)

^c TORAY INDUSTRIES INC   (Japan)

Author keywords

Export switch; Flagella; Morphogenesis; Protein export

Indexed keywords

BACTERIAL PROTEIN; FLGM PROTEIN, BACTERIA;

ARTICLE; BIOSYNTHESIS; CULTURE MEDIUM; ENZYME SPECIFICITY; FLAGELLUM; GENETICS; GROWTH, DEVELOPMENT AND AGING; METABOLISM; PHYSIOLOGY; SALMONELLA TYPHIMURIUM; ULTRASTRUCTURE;

BACTERIAL PROTEINS; CULTURE MEDIA; FLAGELLA; SALMONELLA TYPHIMURIUM; SUBSTRATE SPECIFICITY;

EID: 0033158524     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.1301     Document Type: Article

References (16)

1. Macnab, R. M. Flagella and motility. In “Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed.”, eds. Neidhardt, F. C., Curtiss III, R., Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., Reznikoff, W. S., Riley, M., Schaechter, M., and Umbarger, H. E., ASM Press, Washington, DC, pp. 123-145 (1996).
2. Joys, T. M. The covalent structure of the phase-1 flagellar filament protein of Salmonella typhimurium and its comparison with other flagellins. J. Biol. Chem., 260, 15758-15761 (1985).
3. Homma, M., Kutsukake, K., Hasebe, M., lino, T., and Macnab, R. M. FlgB, FlgC, FlgF and FlgG: A family of structurally related proteins in the flagellar basal body of Salmonella typhimurium. J. Mol. Biol., 211, 465-477 (1990).
4. Homma, M., DeRosier, D. J., and Macnab, R. M. Flagellar hook and hook-associated proteins of Salmonella typhimurium and their relationship to other axial components of the flagellum. J. Mol. Biol., 213, 819-832 (1990).
5. Kutsukake, K. and Doi, H. Nucleotide sequence of the flgD gene of Salmonella typhimurium which is essential for flagellar hook formation. Biochim. Biophys. Acta, 1218, 443-446 (1994).
6. Ohnishi, K., Ohto, Y., Aizawa, A.-I., Macnab, R. M., and lino, T. FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium. J. Bacteriol., 176, 2272-2281 (1994).
7. Hughes, K. T., Gillen, K. L., Semon, M. J., and Karlinsey, J. E. Sensing structural intermediates in bacterial flagellar assembly by export of a negative regulator. Science, 262,1277-1280 (1993).
8. Kutsukake, K. Excretion of the anti-sigma factor through a flagellar substructure couples flagellar gene expression with flagellar assembly in Salmonella typhimurium. Mol. Gen. Genet., 243, 605-612 (1994).
9. Hirano, T., Yamaguchi, S., Oosawa, K., and Aizawa, S.-I. Roles of FliK and FlhB in determination of flagellar hook length in Salmonella typhimurium. J. Bacteriol., 176, 5439-5449 (1994).
10. Kutsukake, K. and lino, T. Role of FliΑ-FlgM regulatory system on the transcriptional control of the flagellar regulon and flagellar formation in Salmonella typhimurium. J. Bacteriol., 176, 3598-3605 (1994).
11. Kutsukake, K., Minamino, T., and Yokoseki, T. Isolation and characterization of FliK-independent flagellation mutants from Salmonella typhimurium. J. Bacteriol., 176, 7625-7629 (1994).
12. Kutsukake, K. Hook-length control of the export-switching machinery involves a double-locked gate in Salmonella typhimurium flagellar morphogenesis. J. Bacteriol., 179, 1268-1273 (1997).
13. Williams, A. W., Yamaguchi, S., Togashi, F., Aizawa, S.-I., Kawagishi, I., and Macnab, R. M. Mutations in fliK and flhB affecting flagellar hook and filament assembly in Salmonella typhimurium. J. Bacteriol, 178, 2960-2970 (1996).
14. Suzuki, T., lino, T., Horiguchi, T., and Yamaguchi, S. Incomplete flagellar structures in nonflagellate mutants of Salmonella typhimurium. J. Bacteriol, 133, 904-915 (1978).
15. Kubori, T., Shimamoto, N., Yamaguchi, S., Namba, K., and Aizawa, S.-I. Morphological pathway of flagellar assembly in Salmonella typhimurium. J. Mol. Biol, 226, 433-446 (1992).
16. Amann, E., Ochs, B., and Abel, K.-J. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene, 69, 301-314 (1988).