메뉴 건너뛰기




Volumn 178, Issue 15, 1996, Pages 4582-4589

Analysis of a FliM-FliN flagellar switch fusion mutant of Salmonella typhimurium

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; FLAGELLUM; GENE DELETION; GENE SEQUENCE; GENETIC ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; SALMONELLA TYPHIMURIUM;

EID: 0029785914     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.15.4582-4589.1996     Document Type: Article
Times cited : (23)

References (42)
  • 1
    • 0021913736 scopus 로고
    • Purification and characterization of the flagellar hook-basal body complex of Salmonella typhimurium
    • Aizawa, S.-I., G. E. Dean, C. J. Jones, R. M. Macnab, and S. Yamaguchi. 1985. Purification and characterization of the flagellar hook-basal body complex of Salmonella typhimurium. J. Bacteriol. 161: 836-849.
    • (1985) J. Bacteriol. , vol.161 , pp. 836-849
    • Aizawa, S.-I.1    Dean, G.E.2    Jones, C.J.3    Macnab, R.M.4    Yamaguchi, S.5
  • 2
    • 0026572085 scopus 로고
    • Correlation between phosphorylation of the chemotaxis protein Che Y and its activity at the flagellar motor
    • Barak, R., and M. Eisenbach. 1992. Correlation between phosphorylation of the chemotaxis protein Che Y and its activity at the flagellar motor. Biochemistry 31: 1821-1826.
    • (1992) Biochemistry , vol.31 , pp. 1821-1826
    • Barak, R.1    Eisenbach, M.2
  • 3
    • 0025021988 scopus 로고
    • Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY
    • Bourret, R. B., J. F. Hess, and M. I. Simon. 1990. Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY. Proc. Natl. Acad. Sci. USA 87: 41-45.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 41-45
    • Bourret, R.B.1    Hess, J.F.2    Simon, M.I.3
  • 4
    • 85035169235 scopus 로고    scopus 로고
    • Personal communication
    • 3a.Blair, D. Personal communication.
    • Blair, D.1
  • 5
    • 0024286468 scopus 로고
    • Bacterial motility: Membrane topology of the Escherichia coli MotB protein
    • Chun, S. Y., and J. S. Parkinson. 1988. Bacterial motility: membrane topology of the Escherichia coli MotB protein. Science 239: 276-278.
    • (1988) Science , vol.239 , pp. 276-278
    • Chun, S.Y.1    Parkinson, J.S.2
  • 6
    • 0021611311 scopus 로고
    • Gene sequence and predicted amino acid sequence of the MotA protein, a membrane-associated protein required for flagellar rotation in Escherichia coli
    • Dean, G. E., R. M. Macnab, J. Stader, P. Matsumura, and C. Burks. 1984. Gene sequence and predicted amino acid sequence of the MotA protein, a membrane-associated protein required for flagellar rotation in Escherichia coli. J. Bacteriol. 159: 991-999.
    • (1984) J. Bacteriol. , vol.159 , pp. 991-999
    • Dean, G.E.1    Macnab, R.M.2    Stader, J.3    Matsumura, P.4    Burks, C.5
  • 7
    • 0028263998 scopus 로고
    • The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both Gram-positive and Gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan
    • De Mot, R., and J. Vanderleyden. 1994. The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both Gram-positive and Gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan. Mol. Microbiol. 12: 333-334.
    • (1994) Mol. Microbiol. , vol.12 , pp. 333-334
    • De Mot, R.1    Vanderleyden, J.2
  • 8
    • 0026740392 scopus 로고
    • Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-ring face of the basal body
    • Francis, N. R., V. M. Irikura, S. Yamaguchi, D. J. DeRosier, and R. M. Macnab. 1992. Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-ring face of the basal body. Proc. Natl. Acad. Sci. USA 89: 6304-6308.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6304-6308
    • Francis, N.R.1    Irikura, V.M.2    Yamaguchi, S.3    DeRosier, D.J.4    Macnab, R.M.5
  • 9
    • 0028274712 scopus 로고
    • Isolation, characterization and structure of bacterial flagellar motors containing the switch complex
    • Francis, N. R., G. E. Sosinsky, D. Thomas, and D. J. DeRosier. 1994. Isolation, characterization and structure of bacterial flagellar motors containing the switch complex. J. Mol. Biol. 235: 1261-1270.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1261-1270
    • Francis, N.R.1    Sosinsky, G.E.2    Thomas, D.3    Derosier, D.J.4
  • 10
    • 0024008340 scopus 로고
    • Identification and characterization of the products of six region III flagellar genes (flaAII.3 through flaQII) of Salmonella typhimurium
    • Homma, M., T. Iino, and R. M. Macnab. 1988. Identification and characterization of the products of six region III flagellar genes (flaAII.3 through flaQII) of Salmonella typhimurium. J. Bacteriol. 170: 2221-2228.
    • (1988) J. Bacteriol. , vol.170 , pp. 2221-2228
    • Homma, M.1    Iino, T.2    Macnab, R.M.3
  • 11
    • 0021812895 scopus 로고
    • Structural genes for flagellar hook-associated proteins in Salmonella typhimurium
    • Homma, M., K. Kutsukake, and T. Iino. 1985. Structural genes for flagellar hook-associated proteins in Salmonella typhimurium. J. Bacteriol. 163: 464-471.
    • (1985) J. Bacteriol. , vol.163 , pp. 464-471
    • Homma, M.1    Kutsukake, K.2    Iino, T.3
  • 12
    • 0027407375 scopus 로고
    • Salmonella typhimurium fliG and flin mutations causing defects in assembly, rotation, and switching of the flagellar motor
    • Irikura, V. M., M. Kihara, S. Yamaguchi, H. Sockett, and R. M. Macnab. 1993. Salmonella typhimurium fliG and fliN mutations causing defects in assembly, rotation, and switching of the flagellar motor. J. Bacteriol. 175: 802-810.
    • (1993) J. Bacteriol. , vol.175 , pp. 802-810
    • Irikura, V.M.1    Kihara, M.2    Yamaguchi, S.3    Sockett, H.4    Macnab, R.M.5
  • 13
    • 0029978352 scopus 로고    scopus 로고
    • Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deepetch replica images
    • Katayama, E., T. Shiraishi, K. Oosawa, N. Baba, and S.-I. Aizawa. 1996. Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deepetch replica images. J. Mol. Biol. 255: 458-475.
    • (1996) J. Mol. Biol. , vol.255 , pp. 458-475
    • Katayama, E.1    Shiraishi, T.2    Oosawa, K.3    Baba, N.4    Aizawa, S.-I.5
  • 14
    • 0023750050 scopus 로고
    • Effects of mot gene expression on the structure of the flagellar motor
    • Khan, S., M. Dapice, and T. S. Reese. 1988. Effects of mot gene expression on the structure of the flagellar motor. J. Mol. Biol. 202: 575-584.
    • (1988) J. Mol. Biol. , vol.202 , pp. 575-584
    • Khan, S.1    Dapice, M.2    Reese, T.S.3
  • 15
    • 0024332574 scopus 로고
    • Flagellar switch of Salmonella typhimurium: Gene sequences and deduced protein sequences
    • Kihara, M., M. Homma, K. Kutsukake, and R. M. Macnab. 1989. Flagellar switch of Salmonella typhimurium: gene sequences and deduced protein sequences. J. Bacteriol 171: 3247-3257.
    • (1989) J. Bacteriol , vol.171 , pp. 3247-3257
    • Kihara, M.1    Homma, M.2    Kutsukake, K.3    Macnab, R.M.4
  • 16
    • 0029092472 scopus 로고
    • Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins
    • Koebnik, R. 1995. Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins. Mol. Microbiol. 16: 1269-1270.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1269-1270
    • Koebnik, R.1
  • 17
    • 0026752989 scopus 로고
    • Morphological pathway of flagellar assembly in Salmonella typhimurium
    • Kubori, T., N. Shimamoto, S. Yamaguchi, K. Namba, and S.-I. Aizawa. 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.-I.5
  • 18
    • 0023116688 scopus 로고
    • Roles of cheY and cHeZ gene products in controlling flagellar rotation in bacterial chemotaxis of Escherichia coli
    • Kuo, S. C., and D. E. Koshland, Jr. 1987. Roles of cheY and cHeZ gene products in controlling flagellar rotation in bacterial chemotaxis of Escherichia coli. J. Bacteriol. 169: 1307-1314.
    • (1987) J. Bacteriol. , vol.169 , pp. 1307-1314
    • Kuo, S.C.1    Koshland Jr., D.E.2
  • 19
    • 0030066344 scopus 로고    scopus 로고
    • Torque generation in the flagellar motor of Escherichia coli: Evidence of a direct role for FliG but not FliM or FliN
    • Lloyd, S. A., H. Tang, X. Wang, S. Billings, and D. F. Blair. 1996. Torque generation in the flagellar motor of Escherichia coli: evidence of a direct role for FliG but not FliM or FliN. J. Bacteriol. 178: 223-231.
    • (1996) J. Bacteriol. , vol.178 , pp. 223-231
    • Lloyd, S.A.1    Tang, H.2    Wang, X.3    Billings, S.4    Blair, D.F.5
  • 20
    • 0025314338 scopus 로고
    • Divalent metal ion binding to the CheY protein and its significance to phosphotransfer in bacterial chemotaxis
    • Lukat, G. S., A. M. Stock, and J. B. Stock. 1990. Divalent metal ion binding to the CheY protein and its significance to phosphotransfer in bacterial chemotaxis. Biochemistry 29: 5436-5442.
    • (1990) Biochemistry , vol.29 , pp. 5436-5442
    • Lukat, G.S.1    Stock, A.M.2    Stock, J.B.3
  • 21
    • 0017132660 scopus 로고
    • Examination of bacterial flagellation by dark-field microscopy
    • Macnab, R. M. 1976. Examination of bacterial flagellation by dark-field microscopy. J. Clin. Microbiol. 4: 258-265.
    • (1976) J. Clin. Microbiol. , vol.4 , pp. 258-265
    • Macnab, R.M.1
  • 22
    • 0002574321 scopus 로고
    • Flagellar switch
    • J. A. Hoch and T. J. Silhavy (ed.), ASM Press, Washington, D.C.
    • Macnab, R. M. 1995. Flagellar switch, p. 181-199. In J. A. Hoch and T. J. Silhavy (ed.), Two-component signal transduction. ASM Press, Washington, D.C.
    • (1995) Two-component Signal Transduction , pp. 181-199
    • Macnab, R.M.1
  • 23
    • 0000887786 scopus 로고    scopus 로고
    • Flagella and motility
    • F. C. Neidhardt, R. Curtiss III, C. A. Gross, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), ASM Press, Washington, D.C.
    • Macnab, R. M. 1996. Flagella and motility, p. 123-145. In F. C. Neidhardt, R. Curtiss III, C. A. Gross, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 123-145
    • Macnab, R.M.1
  • 24
    • 0024594008 scopus 로고
    • DNA sequence analysis, gene product identification, and localization of flagellar motor components of Escherichia coli
    • Malakooti, J., Y. Komeda, and P. Matsumura. 1989. DNA sequence analysis, gene product identification, and localization of flagellar motor components of Escherichia coli. J. Bacteriol. 171: 2728-2734.
    • (1989) J. Bacteriol. , vol.171 , pp. 2728-2734
    • Malakooti, J.1    Komeda, Y.2    Matsumura, P.3
  • 26
    • 0026761084 scopus 로고
    • A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations
    • Roman, S. J., M. Meyers, K. Volz, and P. Matsumura. 1992. A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations. J. Bacteriol. 174: 6247-6255.
    • (1992) J. Bacteriol. , vol.174 , pp. 6247-6255
    • Roman, S.J.1    Meyers, M.2    Volz, K.3    Matsumura, P.4
  • 27
    • 0025059008 scopus 로고
    • Quick transformation in Salmonella typhimurium LT2
    • Ryu, J., and R. J. Hartin. 1990. Quick transformation in Salmonella typhimurium LT2. BioTechniques 8: 43-44.
    • (1990) BioTechniques , vol.8 , pp. 43-44
    • Ryu, J.1    Hartin, R.J.2
  • 28
    • 0026541539 scopus 로고
    • Molecular analysis of the flagellar switch protein FliM of Salmonella typhimurium
    • Sockett, H., S. Yamaguchi, M. Kihara, V. M. Irikura, and R. M. Macnab. 1992. Molecular analysis of the flagellar switch protein FliM of Salmonella typhimurium. J. Bacteriol. 174: 793-806.
    • (1992) J. Bacteriol. , vol.174 , pp. 793-806
    • Sockett, H.1    Yamaguchi, S.2    Kihara, M.3    Irikura, V.M.4    Macnab, R.M.5
  • 29
    • 0022531430 scopus 로고
    • Nucleotide sequence of the Escherichia coli motB gene and site-limited incorporation of its product into the cytoplasmic membrane
    • Stader, J., P. Matsumura, D. Vacante, G. E. Dean, and R. M. Macnab. 1986. Nucleotide sequence of the Escherichia coli motB gene and site-limited incorporation of its product into the cytoplasmic membrane. J. Bacteriol. 166: 244-252.
    • (1986) J. Bacteriol. , vol.166 , pp. 244-252
    • Stader, J.1    Matsumura, P.2    Vacante, D.3    Dean, G.E.4    Macnab, R.M.5
  • 30
    • 0029009964 scopus 로고
    • Regulated underexpression and overexpression of the Flin protein of Escherichia coli and evidence for an interaction between Flin and FliM in the flagellar motor
    • Tang, H., S. Billings, X. Wang, L. Sharp, and D. F. Blair. 1995. Regulated underexpression and overexpression of the FliN protein of Escherichia coli and evidence for an interaction between FliN and FliM in the flagellar motor. J. Bacteriol. 177: 3496-3503.
    • (1995) J. Bacteriol. , vol.177 , pp. 3496-3503
    • Tang, H.1    Billings, S.2    Wang, X.3    Sharp, L.4    Blair, D.F.5
  • 31
    • 0029070133 scopus 로고
    • Regulated underexpression of the FliM protein of Escherichia coli and evidence for a location in the flagellar motor distinct from the MotA/MotB torque generators
    • Tang, H., and D. F. Blair. 1995. Regulated underexpression of the FliM protein of Escherichia coli and evidence for a location in the flagellar motor distinct from the MotA/MotB torque generators. J. Bacteriol. 177: 3485-3495.
    • (1995) J. Bacteriol. , vol.177 , pp. 3485-3495
    • Tang, H.1    Blair, D.F.2
  • 32
    • 0027517812 scopus 로고
    • Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria
    • Welch, M., K. Oosawa, S.-I. Aizawa, and M. Eisenbach. 1993. Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. Proc. Natl. Acad. Sci. USA 90: 8787-8791.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8787-8791
    • Welch, M.1    Oosawa, K.2    Aizawa, S.-I.3    Eisenbach, M.4
  • 33
    • 0028167952 scopus 로고
    • 2+, and conformation of the chemotaxis protein ChcY on its binding to the flagellar switch protein FliM
    • 2+, and conformation of the chemotaxis protein ChcY on its binding to the flagellar switch protein FliM. Biochemistry 33: 10470-10476.
    • (1994) Biochemistry , vol.33 , pp. 10470-10476
    • Welch, M.1    Oosawa, K.2    Aizawa, S.-I.3    Eisenbach, M.4
  • 35
    • 85035169514 scopus 로고    scopus 로고
    • Personal communication
    • 32b.Yamaguchi, S. Personal communication.
    • Yamaguchi, S.1
  • 36
    • 0022899744 scopus 로고
    • Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium
    • Yamaguchi, S., S.-I. Aizawa, M. Kihara, M. Isomura, C. J. Jones, and R. M. Macnab. 1986. Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium. J. Bacteriol. 168: 1172-1179.
    • (1986) J. Bacteriol. , vol.168 , pp. 1172-1179
    • Yamaguchi, S.1    Aizawa, S.-I.2    Kihara, M.3    Isomura, M.4    Jones, C.J.5    Macnab, R.M.6
  • 37
    • 0022454124 scopus 로고
    • Subdivision of flagellar genes of Salmonella typhimurium into regions responsible for assembly, rotation, and switching
    • Yamaguchi, S., H. Fujita, A. Ishihara, S.-I. Aizawa, and R. M. Macnab. 1986. Subdivision of flagellar genes of Salmonella typhimurium into regions responsible for assembly, rotation, and switching. J. Bacteriol. 166: 187-193.
    • (1986) J. Bacteriol. , vol.166 , pp. 187-193
    • Yamaguchi, S.1    Fujita, H.2    Ishihara, A.3    Aizawa, S.-I.4    Macnab, R.M.5
  • 38
    • 0021347115 scopus 로고
    • Genetic analysis of H2, the structural gene for phase-2 flagellin in Salmonella
    • Yamaguchi, S., H. Fujita, K. Sugata, T. Taira, and T. Iino. 1984. Genetic analysis of H2, the structural gene for phase-2 flagellin in Salmonella. J. Gen. Microbiol. 130: 255-265.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 255-265
    • Yamaguchi, S.1    Fujita, H.2    Sugata, K.3    Taira, T.4    Iino, T.5
  • 40
    • 85035163697 scopus 로고    scopus 로고
    • Flin is a major component of the C-ring in the Salmonella typhimurium flagellar basal body
    • in press
    • Zhao, R., N. Pathak, H. Jane, T. S. Reese, and S. Khan. FliN is a major component of the C-ring in the Salmonella typhimurium flagellar basal body. J. Mol. Biol., in press.
    • J. Mol. Biol.
    • Zhao, R.1    Pathak, N.2    Jane, H.3    Reese, T.S.4    Khan, S.5
  • 41
    • 0029091434 scopus 로고
    • Structural effects of mutations in Salmonella typhimurium flagellar switch complex
    • Zhao, R., S. C. Schuster, and S. Khan. 1995. Structural effects of mutations in Salmonella typhimurium flagellar switch complex. J. Mol. Biol. 251: 400-412.
    • (1995) J. Mol. Biol. , vol.251 , pp. 400-412
    • Zhao, R.1    Schuster, S.C.2    Khan, S.3
  • 42
    • 0029165325 scopus 로고
    • Membrane topology of the MotA protein of Escherichia coli
    • Zhou, J., R. T. Fazzio, and D. F. Blair. 1995. Membrane topology of the MotA protein of Escherichia coli. J. Mol. Biol. 251: 237-242.
    • (1995) J. Mol. Biol. , vol.251 , pp. 237-242
    • Zhou, J.1    Fazzio, R.T.2    Blair, D.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.