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Volumn 139, Issue 1, 2006, Pages 113-121

Regulation of polar flagellar number by the flhF and flhG genes in Vibrio alginolyticus

Author keywords

Bacterial flagella; FtsY; MinD; Multiflagellate mutants

Indexed keywords

FLAGELLIN;

EID: 32944458166     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvj010     Document Type: Article
Times cited : (83)

References (54)
  • 1
    • 0000887786 scopus 로고    scopus 로고
    • Flagella and motility
    • (Neidhardt, F.C., ed.), American Society for Microbiology, Washington, DC
    • Macnab, R. (1996) Flagella and motility. In Escherichia coli and Salmonella (Neidhardt, F.C., ed.) pp. 123-145, American Society for Microbiology, Washington, DC
    • (1996) Escherichia Coli and Salmonella , pp. 123-145
    • Macnab, R.1
  • 2
    • 0041664046 scopus 로고    scopus 로고
    • Swarming motility in undomesticated Bacillus subtilis
    • Kearns, D.B. and Losick, R. (2003) Swarming motility in undomesticated Bacillus subtilis. Mol. Microbiol. 49, 581-590
    • (2003) Mol. Microbiol. , vol.49 , pp. 581-590
    • Kearns, D.B.1    Losick, R.2
  • 3
    • 0034744733 scopus 로고    scopus 로고
    • 28-dependent flagellar gene transcription hierarchy of Vibrio cholerae
    • 28-dependent flagellar gene transcription hierarchy of Vibrio cholerae. Mol. Microbiol. 39, 1595-1609
    • (2001) Mol. Microbiol. , vol.39 , pp. 1595-1609
    • Prouty, M.G.1    Correa, N.B.2    Klose, K.E.3
  • 4
    • 0028173998 scopus 로고
    • The expression of asymmetry during Caulobacter cell differentiation
    • Brun, Y.V., Marczynski, G., and Shapiro, L. (1994) The expression of asymmetry during Caulobacter cell differentiation. Annu. Rev. Biochem. 63, 419-450
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 419-450
    • Brun, Y.V.1    Marczynski, G.2    Shapiro, L.3
  • 5
    • 0020679926 scopus 로고
    • Transductional analysis of the flagellar genes in Pseudomonas aeruginosa
    • Tsuda, M. and Iino, T. (1983) Transductional analysis of the flagellar genes in Pseudomonas aeruginosa. J. Bacteriol. 153, 1018-1026
    • (1983) J. Bacteriol. , vol.153 , pp. 1018-1026
    • Tsuda, M.1    Iino, T.2
  • 6
    • 3042611950 scopus 로고    scopus 로고
    • Vibrio fischeri flagellin a is essential for normal motility and for symbiotic competence during initial squid light organ colonization
    • Millikan, D.S. and Ruby, E.G. (2004) Vibrio fischeri flagellin A is essential for normal motility and for symbiotic competence during initial squid light organ colonization. J. Bacteriol. 186, 4315-4325
    • (2004) J. Bacteriol. , vol.186 , pp. 4315-4325
    • Millikan, D.S.1    Ruby, E.G.2
  • 8
    • 0024342933 scopus 로고
    • Flagellation of Pseudomonas putida and analysis of its motile behavior
    • Harwood, C.S., Fosnaugh, K., and Dispensa, M. (1989) Flagellation of Pseudomonas putida and analysis of its motile behavior. J. Bacteriol. 171, 4063-4066
    • (1989) J. Bacteriol. , vol.171 , pp. 4063-4066
    • Harwood, C.S.1    Fosnaugh, K.2    Dispensa, M.3
  • 9
    • 0034828107 scopus 로고    scopus 로고
    • Polar flagellar motility of the Vibrionaceae
    • McCarter, L.L. (2001) Polar flagellar motility of the Vibrionaceae. Microbiol. Mol Biol Rev. 65, 445-462
    • (2001) Microbiol. Mol Biol Rev. , vol.65 , pp. 445-462
    • McCarter, L.L.1
  • 10
    • 0035035298 scopus 로고    scopus 로고
    • Polarity in action: Asymmetric protein localization in bacteria
    • Lybarger, S.R. and Maddock, J.R. (2001) Polarity in action: asymmetric protein localization in bacteria. J. Bacteriol. 183, 3261-3267
    • (2001) J. Bacteriol. , vol.183 , pp. 3261-3267
    • Lybarger, S.R.1    Maddock, J.R.2
  • 11
    • 0037032826 scopus 로고    scopus 로고
    • Generating and exploiting polarity in bacteria
    • Shapiro, L., McAdams, H.H., and Losick, R. (2002) Generating and exploiting polarity in bacteria. Science 298, 1942-1946
    • (2002) Science , vol.298 , pp. 1942-1946
    • Shapiro, L.1    McAdams, H.H.2    Losick, R.3
  • 12
    • 0027272019 scopus 로고
    • Localization of the ActA polypeptide of Listeria monocytogenes in infected tissue culture cell lines: ActA is not associated with actin "comets"
    • Niebuhr, K., Chakraborty, T., Ronde, M., Gazlig, T., Jansen, B., Kollner, P., and Wehland, J. (1993) Localization of the ActA polypeptide of Listeria monocytogenes in infected tissue culture cell lines: ActA is not associated with actin "comets". Infect. Immun. 61, 2793-2802
    • (1993) Infect. Immun. , vol.61 , pp. 2793-2802
    • Niebuhr, K.1    Chakraborty, T.2    Ronde, M.3    Gazlig, T.4    Jansen, B.5    Kollner, P.6    Wehland, J.7
  • 14
    • 1542618323 scopus 로고    scopus 로고
    • Chemoreceptor signaling involves dimer-to-dimer interaction with its cluster at a cell pole
    • Homma, M., Shiomi, D., Homma, M., and Kawagishi, I. (2004) Chemoreceptor signaling involves dimer-to-dimer interaction with its cluster at a cell pole. Proc. Natl. Acad. Sci. USA 101, 3462,-3467
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3462-3467
    • Homma, M.1    Shiomi, D.2    Homma, M.3    Kawagishi, I.4
  • 15
    • 0038349270 scopus 로고    scopus 로고
    • MinD and role of the deviant Walker a motif, dimerization and membrane binding in oscillation
    • Lutkenhaus, J. and Sundaramoorthy, M. (2003) MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation. Mol. Microbiol. 48, 295-303
    • (2003) Mol. Microbiol. , vol.48 , pp. 295-303
    • Lutkenhaus, J.1    Sundaramoorthy, M.2
  • 16
    • 0032743092 scopus 로고    scopus 로고
    • MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli
    • Raskin, D.M. and de Boer, P.A. (1999) MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli. J. Bacteriol. 181, 6419-6424
    • (1999) J. Bacteriol. , vol.181 , pp. 6419-6424
    • Raskin, D.M.1    De Boer, P.A.2
  • 17
    • 0033609139 scopus 로고    scopus 로고
    • Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli
    • Raskin, D.M. and de Boer, P.A. (1999) Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli. Proc. Natl. Acad. Sci. USA 96, 4971-4976
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4971-4976
    • Raskin, D.M.1    De Boer, P.A.2
  • 18
    • 0030906717 scopus 로고    scopus 로고
    • Regulation of the Caulobacter flagellar gene hierarchy; not just for motility
    • Wu, J. and Newton, A. (1997) Regulation of the Caulobacter flagellar gene hierarchy; not just for motility. Mol. Microbiol. 24, 233-239
    • (1997) Mol. Microbiol. , vol.24 , pp. 233-239
    • Wu, J.1    Newton, A.2
  • 19
    • 0034046746 scopus 로고    scopus 로고
    • Analysis of the polar flagellar gene system of Vibrio parahaemolyticus
    • Kim, Y.K. and McCarter, L.L. (2000) Analysis of the polar flagellar gene system of Vibrio parahaemolyticus. J. Bacteriol. 182, 3693-3704
    • (2000) J. Bacteriol. , vol.182 , pp. 3693-3704
    • Kim, Y.K.1    McCarter, L.L.2
  • 20
    • 0026752989 scopus 로고
    • Morphological pathway of flagellar assembly in Salmonella typhimurium
    • Kubori, T., Shimamoto, N., Yamaguchi, S., Namba, K., and Aizawa, S. (1992) Morphological pathway of flagellar assembly in Salmonella typhimurium. J. Mol. Biol. 226, 433-446
    • (1992) J. Mol. Biol. , vol.226 , pp. 433-446
    • Kubori, T.1    Shimamoto, N.2    Yamaguchi, S.3    Namba, K.4    Aizawa, S.5
  • 21
    • 0033624769 scopus 로고    scopus 로고
    • The G-protein FlhF has a role in polar flagellar placement and general stress response induction in Pseudomonas putida
    • Pandza, S., Baetens, M., Park, C.H., Au, T., Keyhan, M., and Matin, A. (2000) The G-protein FlhF has a role in polar flagellar placement and general stress response induction in Pseudomonas putida. Mol. Microbiol. 36, 414-423
    • (2000) Mol. Microbiol. , vol.36 , pp. 414-423
    • Pandza, S.1    Baetens, M.2    Park, C.H.3    Au, T.4    Keyhan, M.5    Matin, A.6
  • 22
    • 0342980432 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa motR gene involved in regulation of bacterial motility
    • Campos-Garcia, J., Najera, R., Camarena, L., and Soberon-Chavez, G. (2000) The Pseudomonas aeruginosa motR gene involved in regulation of bacterial motility. FEMS Microbiol. Lett. 184, 57-62
    • (2000) FEMS Microbiol. Lett. , vol.184 , pp. 57-62
    • Campos-Garcia, J.1    Najera, R.2    Camarena, L.3    Soberon-Chavez, G.4
  • 23
    • 0033987999 scopus 로고    scopus 로고
    • FleN, a gene that regulates flagellar number in Pseudomonas aeruginosa
    • Dasgupta, N., Arora, S.K., and Ramphal, R. (2000) fleN, a gene that regulates flagellar number in Pseudomonas aeruginosa. J. Bacteriol. 182, 357-364
    • (2000) J. Bacteriol. , vol.182 , pp. 357-364
    • Dasgupta, N.1    Arora, S.K.2    Ramphal, R.3
  • 24
    • 0034748979 scopus 로고    scopus 로고
    • Interaction of the antiactivator FleN with the transcriptional activator FleQ regulates flagellar number in Pseudomonas aeruginosa
    • Dasgupta, N. and Ramphal, R. (2001) Interaction of the antiactivator FleN with the transcriptional activator FleQ regulates flagellar number in Pseudomonas aeruginosa. J. Bacteriol. 183, 6636-6644
    • (2001) J. Bacteriol. , vol.183 , pp. 6636-6644
    • Dasgupta, N.1    Ramphal, R.2
  • 25
    • 0242521414 scopus 로고    scopus 로고
    • A four-tiered transcriptional regulatory circuit controls flagellar biogenesis in Pseudomonas aeruginosa
    • Dasgupta, N., Wolfgang, M.C., Goodman, A.L., Arora, S.K., Jyot, J., Lory, S., and Ramphal, R. (2003) A four-tiered transcriptional regulatory circuit controls flagellar biogenesis in Pseudomonas aeruginosa. Mol. Microbiol. 50, 809-824
    • (2003) Mol. Microbiol. , vol.50 , pp. 809-824
    • Dasgupta, N.1    Wolfgang, M.C.2    Goodman, A.L.3    Arora, S.K.4    Jyot, J.5    Lory, S.6    Ramphal, R.7
  • 26
    • 0015090808 scopus 로고
    • Structure and arrangement of flagella in species of the genus Beneckea and Photobacterium fischen
    • Allen, R.D. and Baumann, P. (1971) Structure and arrangement of flagella in species of the genus Beneckea and Photobacterium fischen. J Bacteriol. 107, 295-302
    • (1971) J Bacteriol. , vol.107 , pp. 295-302
    • Allen, R.D.1    Baumann, P.2
  • 27
    • 0026614338 scopus 로고
    • Polar and lateral flagellar motors of marine Vibrio are driven by different ion-motive forces
    • Atsumi, T., McCarter, L., and Imae, Y. (1992) Polar and lateral flagellar motors of marine Vibrio are driven by different ion-motive forces. Nature 355, 182-184
    • (1992) Nature , vol.355 , pp. 182-184
    • Atsumi, T.1    McCarter, L.2    Imae, Y.3
  • 28
    • 0029143022 scopus 로고
    • Isolation of the polar and lateral flagellum-defective mutants in Vibrio alginolyticus and identification of their flagellar driving energy sources
    • Kawagishi, I., Maekawa, Y., Atsumi, T., Homma, M., and Imae, Y. (1995) Isolation of the polar and lateral flagellum-defective mutants in Vibrio alginolyticus and identification of their flagellar driving energy sources. J. Bacteriol. 177, 5158-5160
    • (1995) J. Bacteriol. , vol.177 , pp. 5158-5160
    • Kawagishi, I.1    Maekawa, Y.2    Atsumi, T.3    Homma, M.4    Imae, Y.5
  • 30
    • 0029955266 scopus 로고    scopus 로고
    • The sodium-driven polar flagellar motor of marine Vibrio as the mechanosensor that regulates lateral flagellar expression
    • Kawagishi, I., Imagawa, M., Imae, Y., McCarter, L., and Homma, M. (1996) The sodium-driven polar flagellar motor of marine Vibrio as the mechanosensor that regulates lateral flagellar expression. Mol. Microbiol. 20, 693-699
    • (1996) Mol. Microbiol. , vol.20 , pp. 693-699
    • Kawagishi, I.1    Imagawa, M.2    Imae, Y.3    McCarter, L.4    Homma, M.5
  • 31
    • 0029919952 scopus 로고    scopus 로고
    • Cloning and characterization of motY, a gene coding for a component of the sodium-driven flagellar motor in Vibrio alginolyticus
    • Okunishi, I., Kawagishi, I., and Homma, M. (1996) Cloning and characterization of motY, a gene coding for a component of the sodium-driven flagellar motor in Vibrio alginolyticus. J. Bacteriol. 178, 2409-2415
    • (1996) J. Bacteriol. , vol.178 , pp. 2409-2415
    • Okunishi, I.1    Kawagishi, I.2    Homma, M.3
  • 32
    • 0031053516 scopus 로고    scopus 로고
    • Vibrio alginolyticus mutants resistant to phenamil, a specific inhibitor of the sodium-driven flagellar motor
    • Kojima, S., Atsumi, T., Muramoto, K., Kudo, S., Kawagishi, I., and Homma, M. (1997) Vibrio alginolyticus mutants resistant to phenamil, a specific inhibitor of the sodium-driven flagellar motor. J. Mol. Biol. 265, 310-318
    • (1997) J. Mol. Biol. , vol.265 , pp. 310-318
    • Kojima, S.1    Atsumi, T.2    Muramoto, K.3    Kudo, S.4    Kawagishi, I.5    Homma, M.6
  • 34
    • 0023229538 scopus 로고
    • Identification and characterization of flagellar hook and basal-body gene products (FlaFV, FlaVI, FlaFVII and FlaFVIII) in Salmonella typhimurium
    • Homma, M., Ohnishi, K., Iino, T., and Macnab, R.M. (1987) Identification and characterization of flagellar hook and basal-body gene products (FlaFV, FlaVI, FlaFVII and FlaFVIII) in Salmonella typhimurium. J. Bacteriol. 169, 3617-3624
    • (1987) J. Bacteriol. , vol.169 , pp. 3617-3624
    • Homma, M.1    Ohnishi, K.2    Iino, T.3    Macnab, R.M.4
  • 35
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose pBAD promoter
    • Guzman, L.M., Belin, D., Carson, M.J., and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose pBAD promoter. J. Bacteriol. 177, 4121-1130
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-11130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 36
    • 0028040922 scopus 로고
    • Removal of the periplasmic DNase before electroporation enhances efficiency of transformation in a marine bacterium Vibrio alginolyticus
    • Kawagishi, I., Okunishi, I., Homma, M., and Imae, Y. (1994) Removal of the periplasmic DNase before electroporation enhances efficiency of transformation in a marine bacterium Vibrio alginolyticus. Microbiology 140, 2355-2361
    • (1994) Microbiology , vol.140 , pp. 2355-2361
    • Kawagishi, I.1    Okunishi, I.2    Homma, M.3    Imae, Y.4
  • 37
    • 0031779435 scopus 로고    scopus 로고
    • Flagellin-containing membrane vesicles excreted from Vibrio alginolyticus mutants lacking a polar-flagellar filament
    • Nishioka, N., Furuno, M., Kawagishi, I., and Homma, M. (1998) Flagellin-containing membrane vesicles excreted from Vibrio alginolyticus mutants lacking a polar-flagellar filament. J. Biochem. 123, 1169-1173
    • (1998) J. Biochem. , vol.123 , pp. 1169-1173
    • Nishioka, N.1    Furuno, M.2    Kawagishi, I.3    Homma, M.4
  • 41
    • 85041115207 scopus 로고    scopus 로고
    • New prospects in studying the bacterial signal recognition particle pathway
    • Herskovits, A.A., Bochkareva, E.S., and Bibi, E. (2000) New prospects in studying the bacterial signal recognition particle pathway. Mol. Microbiol. 38, 927-939
    • (2000) Mol. Microbiol. , vol.38 , pp. 927-939
    • Herskovits, A.A.1    Bochkareva, E.S.2    Bibi, E.3
  • 42
    • 0035201578 scopus 로고    scopus 로고
    • Protein traffic in bacteria: Multiple routes from the ribosome to and across the membrane
    • Muller, M., Koch, H.G., Beck, K., and Schafer, U. (2001) Protein traffic in bacteria: multiple routes from the ribosome to and across the membrane. Prog. Nucleic Acid Res. Mol. Biol. 66, 107-157
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.66 , pp. 107-157
    • Muller, M.1    Koch, H.G.2    Beck, K.3    Schafer, U.4
  • 44
    • 0347584006 scopus 로고    scopus 로고
    • Substrate twinning activates the signal recognition particle and its receptor
    • Egea, P.F., Shan, S.O., Napetschnig, J., Savage, D.F., Walter, P., and Stroud, R.M. (2004) Substrate twinning activates the signal recognition particle and its receptor. Nature 427, 215-221
    • (2004) Nature , vol.427 , pp. 215-221
    • Egea, P.F.1    Shan, S.O.2    Napetschnig, J.3    Savage, D.F.4    Walter, P.5    Stroud, R.M.6
  • 45
    • 0034808131 scopus 로고    scopus 로고
    • The conformation of bound GMPPNP suggests a mechanism for gating the active site of the SRP GTPase
    • Padmanabhan, S. and Freymann, D.M. (2001) The conformation of bound GMPPNP suggests a mechanism for gating the active site of the SRP GTPase. Structure 9, 859-867
    • (2001) Structure , vol.9 , pp. 859-867
    • Padmanabhan, S.1    Freymann, D.M.2
  • 46
    • 0342420593 scopus 로고    scopus 로고
    • Bacterial cell division: A moving MinE sweeper boggles the MinD bacterial division: Finding the dividing line
    • Margolin, W., Sullivan, S.M., and Maddock, J.R. (2001) Bacterial cell division: a moving MinE sweeper boggles the MinD bacterial division: Finding the dividing line. Curr. Biol. 11, 395-398
    • (2001) Curr. Biol. , vol.11 , pp. 395-398
    • Margolin, W.1    Sullivan, S.M.2    Maddock, J.R.3
  • 47
    • 0034704904 scopus 로고    scopus 로고
    • Bacterial division: Finding the dividing line
    • Sullivan, S.M. and Maddock, J.R. (2000) Bacterial division: Finding the dividing line. Curr. Biol. 10, 249-252
    • (2000) Curr. Biol. , vol.10 , pp. 249-252
    • Sullivan, S.M.1    Maddock, J.R.2
  • 48
    • 4344605015 scopus 로고    scopus 로고
    • FlhF, the third signal recognition particle-GTPase of Bacillus subtilis, is dispensable for protein secretion
    • Zanen, G., Antelmann, H., Westers, H., Hecker, M., van Dijl, J.M., and Quax, W.J. (2004) FlhF, the third signal recognition particle-GTPase of Bacillus subtilis, is dispensable for protein secretion. J. Bacteriol. 186, 5956-5960
    • (2004) J. Bacteriol. , vol.186 , pp. 5956-5960
    • Zanen, G.1    Antelmann, H.2    Westers, H.3    Hecker, M.4    Van Dijl, J.M.5    Quax, W.J.6
  • 49
    • 0037699937 scopus 로고    scopus 로고
    • Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles
    • Shih, Y.L., Le, T., and Rothfield, L. (2003) Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles. Proc. Natl. Acad. Sci. USA 100, 7865-7870
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7865-7870
    • Shih, Y.L.1    Le, T.2    Rothfield, L.3
  • 50
    • 0038444526 scopus 로고    scopus 로고
    • Membrane binding by MinD involves insertion of hydrophobic residues within the C-terminal amphipathic helix into the bilayer
    • Zhou, H. and Lutkenhaus, J. (2003) Membrane binding by MinD involves insertion of hydrophobic residues within the C-terminal amphipathic helix into the bilayer. J. Bacteriol. 185, 4326-4335
    • (2003) J. Bacteriol. , vol.185 , pp. 4326-4335
    • Zhou, H.1    Lutkenhaus, J.2
  • 52
    • 0030700668 scopus 로고    scopus 로고
    • Cloning of a Vibrio alginolyticus rpoN gene that is required for polar flagellar formation
    • Kawagishi, I., Nakada, M., Nishioka, N., and Homma, M. (1997) Cloning of a Vibrio alginolyticus rpoN gene that is required for polar flagellar formation. J. Bacteriol. 179, 6851-6854
    • (1997) J. Bacteriol. , vol.179 , pp. 6851-6854
    • Kawagishi, I.1    Nakada, M.2    Nishioka, N.3    Homma, M.4
  • 54
    • 0035831155 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell division regulator MinD
    • Cordell, S.C. and Lowe, J. (2001) Crystal structure of the bacterial cell division regulator MinD. FEBS Lett. 492, 160-165
    • (2001) FEBS Lett. , vol.492 , pp. 160-165
    • Cordell, S.C.1    Lowe, J.2


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