메뉴 건너뛰기




Volumn 13, Issue 7, 2012, Pages 9225-9239

Bacterial motility measured by a miniature chamber for high-pressure microscopy

Author keywords

Bacterial motility; Flagellar motor; High pressure microscopy

Indexed keywords

ARTICLE; BACTERIAL FLAGELLUM; BACTERIAL MOTILITY; BACTERIAL PHENOMENA AND FUNCTIONS; CELL MOTILITY; ESCHERICHIA COLI; HIGH PRESSURE MICROSCOPY; MICROSCOPY; NONHUMAN; PRESSURE; TEMPERATURE; CYTOLOGY; HYDROSTATIC PRESSURE; PHYSIOLOGY;

EID: 84864365985     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms13079225     Document Type: Article
Times cited : (26)

References (91)
  • 1
    • 77957033258 scopus 로고    scopus 로고
    • Gene expression under high pressure
    • Kato, C.; Horikoshi, K. Gene expression under high pressure. Prog. Biotechnol. 1996, 13, 59-66.
    • (1996) Prog. Biotechnol , vol.13 , pp. 59-66
    • Kato, C.1    Horikoshi, K.2
  • 2
    • 84055187752 scopus 로고    scopus 로고
    • Effects of pressure and temperature on the binding of RecA protein to single-stranded DNA
    • Merrin, J.; Kumar, P.; Libchaber, A. Effects of pressure and temperature on the binding of RecA protein to single-stranded DNA. Proc. Natl. Acad. Sci. USA 2011, 108, 19913-19918.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 19913-19918
    • Merrin, J.1    Kumar, P.2    Libchaber, A.3
  • 3
    • 0031980181 scopus 로고    scopus 로고
    • Extremely barophilic bacteria isolated from the Mariana Trench, Challenger Deep, at a depth of 11,000 meters
    • Kato, C.; Li, L.; Nogi, Y.; Nakamura, Y.; Tamaoka, J.; Horikoshi, K. Extremely barophilic bacteria isolated from the Mariana Trench, Challenger Deep, at a depth of 11,000 meters. Appl. Environ. Microbiol. 1998, 64, 1510-1513.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 1510-1513
    • Kato, C.1    Li, L.2    Nogi, Y.3    Nakamura, Y.4    Tamaoka, J.5    Horikoshi, K.6
  • 4
    • 0037171156 scopus 로고    scopus 로고
    • Pressure effects on in vivo microbial processes
    • Bartlett, D.H. Pressure effects on in vivo microbial processes. BBA-Protein Struct M. 2002, 1595, 367-381.
    • (2002) BBA-Protein Struct M , vol.1595 , pp. 367-381
    • Bartlett, D.H.1
  • 5
    • 0022097021 scopus 로고
    • Pressure-induced changes in Ca2+-channel excitability in Paramecium
    • Otter, T.; Salmon, E.D. Pressure-induced changes in Ca2+-channel excitability in Paramecium. J. exp. biol. 1985, 117, 29-43.
    • (1985) J. Exp. Biol , vol.117 , pp. 29-43
    • Otter, T.1    Salmon, E.D.2
  • 6
    • 36148983058 scopus 로고    scopus 로고
    • Exploration of the effects of high hydrostatic pressure on microbial growth, physiology and survival: Perspectives from piezophysiology
    • Abe, F. Exploration of the effects of high hydrostatic pressure on microbial growth, physiology and survival: perspectives from piezophysiology. Biosci. Biotechnol. Biochem. 2007, 71, 2347-2357.
    • (2007) Biosci. Biotechnol. Biochem , vol.71 , pp. 2347-2357
    • Abe, F.1
  • 7
    • 0016732396 scopus 로고
    • Functional organization of mitotic microtubules. Physical chemistry of the in vivo equilibrium system
    • Inoue, S, Fuseler, J, Salmon, E.D, Ellis, G.W. Functional organization of mitotic microtubules. Physical chemistry of the in vivo equilibrium system. Biophys. J. 1975, 15, 725-744.
    • (1975) Biophys. J , vol.15 , pp. 725-744
    • Inoue, S.1    Fuseler, J.2    Salmon, E.D.3    Ellis, G.W.4
  • 8
    • 33644654599 scopus 로고    scopus 로고
    • Microscopy under pressure-an optical chamber system for fluorescence microscopic analysis of living cells under high hydrostatic pressure
    • Frey, B.; Hartmann, M.; Herrmann, M.; Meyer-Pittroff, R.; Sommer, K.; Bluemelhuber, G. Microscopy under pressure-an optical chamber system for fluorescence microscopic analysis of living cells under high hydrostatic pressure. Microsc. Res. Tech. 2006, 69, 65-72.
    • (2006) Microsc. Res. Tech , vol.69 , pp. 65-72
    • Frey, B.1    Hartmann, M.2    Herrmann, M.3    Meyer-Pittroff, R.4    Sommer, K.5    Bluemelhuber, G.6
  • 9
    • 0025678599 scopus 로고
    • Hydrostatic compression in glycerinated rabbit muscle fibers
    • Ranatunga, K.W.; Fortune, N.S.; Geeves, M.A. Hydrostatic compression in glycerinated rabbit muscle fibers. Biophys. J. 1990, 58, 1401-1410.
    • (1990) Biophys. J , vol.58 , pp. 1401-1410
    • Ranatunga, K.W.1    Fortune, N.S.2    Geeves, M.A.3
  • 10
    • 33646869675 scopus 로고    scopus 로고
    • Prolonged high-pressure treatments in mammalian skeletal muscle result in loss of functional sodium channels and altered calcium channel kinetics
    • Friedrich, O.; Kress, K.R.; Hartmann, M.; Frey, B.; Sommer, K.; Ludwig, H.; Fink, R.H. Prolonged high-pressure treatments in mammalian skeletal muscle result in loss of functional sodium channels and altered calcium channel kinetics. Cell Biochem. Biophys. 2006, 45, 71-83.
    • (2006) Cell Biochem. Biophys , vol.45 , pp. 71-83
    • Friedrich, O.1    Kress, K.R.2    Hartmann, M.3    Frey, B.4    Sommer, K.5    Ludwig, H.6    Fink, R.H.7
  • 11
    • 0000072283 scopus 로고
    • Growth, reproduction, and death rates of Escherichia coli at increased hydrostatic pressures
    • Zobell, C.E.; Cobet, A.B. Growth, reproduction, and death rates of Escherichia coli at increased hydrostatic pressures. J. Bacteriol. 1962, 84, 1228-1236.
    • (1962) J. Bacteriol , vol.84 , pp. 1228-1236
    • Zobell, C.E.1    Cobet, A.B.2
  • 12
    • 0027370350 scopus 로고
    • Stress response of Escherichia coli to elevated hydrostatic pressure
    • Welch, T.J.; Farewell, A.; Neidhardt, F.C.; Bartlett, D.H. Stress response of Escherichia coli to elevated hydrostatic pressure. J. Bacteriol. 1993, 175, 7170-7177.
    • (1993) J. Bacteriol , vol.175 , pp. 7170-7177
    • Welch, T.J.1    Farewell, A.2    Neidhardt, F.C.3    Bartlett, D.H.4
  • 13
    • 3142751277 scopus 로고    scopus 로고
    • Effects of high hydrostatic pressure on bacterial cytoskeleton FtsZ polymers in vivo and in vitro
    • Ishii, A.; Sato, T.; Wachi, M.; Nagai, K.; Kato, C. Effects of high hydrostatic pressure on bacterial cytoskeleton FtsZ polymers in vivo and in vitro. Microbiology 2004, 150, 1965-1972.
    • (2004) Microbiology , vol.150 , pp. 1965-1972
    • Ishii, A.1    Sato, T.2    Wachi, M.3    Nagai, K.4    Kato, C.5
  • 14
    • 77952968436 scopus 로고    scopus 로고
    • A multipurpose modular system for high-resolution microscopy at high hydrostatic pressure
    • Vass, H.; Black, S.L.; Herzig, E.M.; Ward, F.B.; Clegg, P.S.; Allen, R.J. A multipurpose modular system for high-resolution microscopy at high hydrostatic pressure. Rev. Sci. Instrum. 2010, 81, 053710.
    • (2010) Rev. Sci. Instrum , vol.81 , pp. 053710
    • Vass, H.1    Black, S.L.2    Herzig, E.M.3    Ward, F.B.4    Clegg, P.S.5    Allen, R.J.6
  • 15
    • 12144286210 scopus 로고    scopus 로고
    • Morphological and physiological changes induced by high hydrostatic pressure in exponential- and stationary-phase cells of Escherichia coli: Relationship with cell death
    • Manas, P.; Mackey, B.M. Morphological and physiological changes induced by high hydrostatic pressure in exponential- and stationary-phase cells of Escherichia coli: Relationship with cell death. Appl. Environ. Microbiol. 2004, 70, 1545-1554.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 1545-1554
    • Manas, P.1    Mackey, B.M.2
  • 16
    • 2142643679 scopus 로고    scopus 로고
    • SulA-independent filamentation of Escherichia coli during growth after release from high hydrostatic pressure treatment
    • Kawarai, T.; Wachi, M.; Ogino, H.; Furukawa, S.; Suzuki, K.; Ogihara, H.; Yamasaki, M. SulA-independent filamentation of Escherichia coli during growth after release from high hydrostatic pressure treatment. Appl. Microbiol. Biotechnol. 2004, 64, 255-262.
    • (2004) Appl. Microbiol. Biotechnol , vol.64 , pp. 255-262
    • Kawarai, T.1    Wachi, M.2    Ogino, H.3    Furukawa, S.4    Suzuki, K.5    Ogihara, H.6    Yamasaki, M.7
  • 17
    • 35448979485 scopus 로고    scopus 로고
    • Damage in Escherichia coli cells treated with a combination of high hydrostatic pressure and subzero temperature
    • Moussa, M.; Perrier-Cornet, J.M.; Gervais, P. Damage in Escherichia coli cells treated with a combination of high hydrostatic pressure and subzero temperature. Appl. Environ. Microbiol. 2007, 73, 6508-6518.
    • (2007) Appl. Environ. Microbiol , vol.73 , pp. 6508-6518
    • Moussa, M.1    Perrier-Cornet, J.M.2    Gervais, P.3
  • 18
    • 0037171130 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy in high-pressure studies on proteins
    • Dzwolak, W.; Kato, M.; Taniguchi, Y. Fourier transform infrared spectroscopy in high-pressure studies on proteins. BBA-Protein Struct M. 2002, 1595, 131-144.
    • (2002) BBA-Protein Struct M , vol.1595 , pp. 131-144
    • Dzwolak, W.1    Kato, M.2    Taniguchi, Y.3
  • 19
    • 3342936435 scopus 로고    scopus 로고
    • High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins
    • Kamatari, Y.O.; Kitahara, R.; Yamada, H.; Yokoyama, S.; Akasaka, K. High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins. Methods 2004, 34, 133-143.
    • (2004) Methods , vol.34 , pp. 133-143
    • Kamatari, Y.O.1    Kitahara, R.2    Yamada, H.3    Yokoyama, S.4    Akasaka, K.5
  • 20
    • 0037171184 scopus 로고    scopus 로고
    • Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure
    • Winter, R. Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure. BBA-Protein Struct M. 2002, 1595, 160-184.
    • (2002) BBA-Protein Struct M , vol.1595 , pp. 160-184
    • Winter, R.1
  • 22
    • 71649088248 scopus 로고    scopus 로고
    • Elastic incoherent neutron scattering as a probe of high pressure induced changes in protein flexibility
    • Filabozzi, A.; Deriu, A.; di Bari, M.T.; Russo, D.; Croci, S.; di Venere, A. Elastic incoherent neutron scattering as a probe of high pressure induced changes in protein flexibility. Biochim. Biophys. Acta 2010, 1804, 63-67.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 63-67
    • Filabozzi, A.1    Deriu, A.2    Di Bari, M.T.3    Russo, D.4    Croci, S.5    Di Venere, A.6
  • 23
    • 33646490977 scopus 로고    scopus 로고
    • High pressure macromolecular crystallography: The 140-MPa crystal structure at 2.3 angstrom resolution of urate oxidase, a 135-kDa tetrameric assembly
    • Colloc'h, N.; Girard, E.; Dhaussy, A.C.; Kahn, R.; Ascone, I.; Mezouar, M.; Fourme, R. High pressure macromolecular crystallography: The 140-MPa crystal structure at 2.3 angstrom resolution of urate oxidase, a 135-kDa tetrameric assembly. BBA-Proteins Proteom. 2006, 1764, 391-397.
    • (2006) BBA-Proteins Proteom , vol.1764 , pp. 391-397
    • Colloc'h, N.1    Girard, E.2    Dhaussy, A.C.3    Kahn, R.4    Ascone, I.5    Mezouar, M.6    Fourme, R.7
  • 24
    • 84855726939 scopus 로고
    • Eicosapentaenoic acid plays a role in stabilizing dynamic membrane structure in the deep-sea piezophile Shewanella violacea: A study employing high-pressure time-resolved fluorescence anisotropy measurement
    • Usui, K.; Hiraki, T.; Kawamoto, J.; Kurihara, T.; Nogi, Y.; Kato, C.; Abe, F. Eicosapentaenoic acid plays a role in stabilizing dynamic membrane structure in the deep-sea piezophile Shewanella violacea: A study employing high-pressure time-resolved fluorescence anisotropy measurement. BBA-Biomembranes 2012, 1818, 574-583.
    • (1818) BBA-Biomembranes , vol.2012 , pp. 574-583
    • Usui, K.1    Hiraki, T.2    Kawamoto, J.3    Kurihara, T.4    Nogi, Y.5    Kato, C.6    Abe, F.7
  • 25
    • 0016693736 scopus 로고
    • A new miniature hydrostatic pressure chamber for microscopy. Strain- free optical glass windows facilitate phase-contrast and polarized-light microscopy of living cells. Optional fixture permits simultaneous control of pressure and temperature
    • Salmon, E.D.; Ellis, G.W. A new miniature hydrostatic pressure chamber for microscopy. Strain- free optical glass windows facilitate phase-contrast and polarized-light microscopy of living cells. Optional fixture permits simultaneous control of pressure and temperature. J. Cell Biol. 1975, 65, 587-602.
    • (1975) J. Cell Biol , vol.65 , pp. 587-602
    • Salmon, E.D.1    Ellis, G.W.2
  • 26
    • 33745475774 scopus 로고    scopus 로고
    • A high-temperature and -pressure microscope cell to observe colloidal behaviors in subcritical and supercritical water Brownian Motion of Colloids Near a Wall
    • Mukai, S.A.; Deguchi, S.; Tsujii, K. A high-temperature and -pressure microscope cell to observe colloidal behaviors in subcritical and supercritical water: Brownian motion of colloids near a wall. Colloid Surface A. 2006, 282, 483-488.
    • (2006) Colloid Surface A , vol.282 , pp. 483-488
    • Mukai, S.A.1    Deguchi, S.2    Tsujii, K.3
  • 27
    • 61549097504 scopus 로고    scopus 로고
    • Pressure-induced changes in the structure and function of the kinesin-microtubule complex
    • Nishiyama, M.; Kimura, Y.; Nishiyama, Y.; Terazima, M. Pressure-induced changes in the structure and function of the kinesin-microtubule complex. Biophys. J. 2009, 96, 1142-1150.
    • (2009) Biophys. J , vol.96 , pp. 1142-1150
    • Nishiyama, M.1    Kimura, Y.2    Nishiyama, Y.3    Terazima, M.4
  • 29
    • 84859917070 scopus 로고    scopus 로고
    • Microscopic analysis of bacterial motility at high pressure
    • Nishiyama, M.; Sowa, M. Microscopic analysis of bacterial motility at high pressure. Biophys. J. 2012, 102, 1872-1880.
    • (2012) Biophys. J , vol.102 , pp. 1872-1880
    • Nishiyama, M.1    Sowa, M.2
  • 30
    • 37749029507 scopus 로고    scopus 로고
    • Bacterial chemoreceptors: High-performance signaling in networked arrays
    • Hazelbauer, G.L.; Falke, J.J.; Parkinson, J.S. Bacterial chemoreceptors: high-performance signaling in networked arrays. Trends Biochem. Sci. 2008, 33, 9-19.
    • (2008) Trends Biochem. Sci , vol.33 , pp. 9-19
    • Hazelbauer, G.L.1    Falke, J.J.2    Parkinson, J.S.3
  • 32
    • 34548356914 scopus 로고    scopus 로고
    • Aer on the inside looking out: Paradigm for a PAS-HAMP role in sensing oxygen, redox and energy
    • Taylor, B.L. Aer on the inside looking out: paradigm for a PAS-HAMP role in sensing oxygen, redox and energy. Mol. Microbiol. 2007, 65, 1415-1424.
    • (2007) Mol. Microbiol , vol.65 , pp. 1415-1424
    • Taylor, B.L.1
  • 33
    • 0029114533 scopus 로고
    • Phototaxis away from blue light by an Escherichia coli mutant accumulating protoporphyrin IX
    • Yang, H.; Inokuchi, H.; Adler, J. Phototaxis away from blue light by an Escherichia coli mutant accumulating protoporphyrin IX. Proc. Natl. Acad. Sci. USA 1995, 92, 7332-7336.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7332-7336
    • Yang, H.1    Inokuchi, H.2    Adler, J.3
  • 34
    • 0017106309 scopus 로고
    • Effect of temperature on motility and chemotaxis of Escherichia coli
    • Maeda, K.; Imae, Y.; Shioi, J.I.; Oosawa, F. Effect of temperature on motility and chemotaxis of Escherichia coli. J. Bacteriol. 1976, 127, 1039-1046.
    • (1976) J. Bacteriol , vol.127 , pp. 1039-1046
    • Maeda, K.1    Imae, Y.2    Shioi, J.I.3    Oosawa, F.4
  • 35
    • 0345677855 scopus 로고    scopus 로고
    • Conversion of a bacterial warm sensor to a cold sensor by methylation of a single residue in the presence of an attractant
    • Nishiyama, S.I.; Umemura, T.; Nara, T.; Homma, M.; Kawagishi, I. Conversion of a bacterial warm sensor to a cold sensor by methylation of a single residue in the presence of an attractant. Mol. Microbiol. 1999, 32, 357-365.
    • (1999) Mol. Microbiol , vol.32 , pp. 357-365
    • Nishiyama, S.I.1    Umemura, T.2    Nara, T.3    Homma, M.4    Kawagishi, I.5
  • 36
    • 0033548704 scopus 로고    scopus 로고
    • Inversion of thermosensing property of the bacterial receptor Tar by mutations in the second transmembrane region
    • Nishiyama, S.; Maruyama, I.N.; Homma, M.; Kawagishi, I. Inversion of thermosensing property of the bacterial receptor Tar by mutations in the second transmembrane region. J. Mol. Biol. 1999, 286, 1275-1284.
    • (1999) J. Mol. Biol , vol.286 , pp. 1275-1284
    • Nishiyama, S.1    Maruyama, I.N.2    Homma, M.3    Kawagishi, I.4
  • 37
    • 34548311951 scopus 로고    scopus 로고
    • A concentration-dependent switch in the bacterial response to temperature
    • Salman, H.; Libchaber, A. A concentration-dependent switch in the bacterial response to temperature. Nat. Cell Biol. 2007, 9, 1098-1100.
    • (2007) Nat. Cell Biol , vol.9 , pp. 1098-1100
    • Salman, H.1    Libchaber, A.2
  • 38
    • 44449155725 scopus 로고    scopus 로고
    • The thermal impulse response of Escherichia coli
    • Paster, E.; Ryu, W.S. The thermal impulse response of Escherichia coli. Proc. Natl. Acad. Sci. USA 2008, 105, 5373-5377.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5373-5377
    • Paster, E.1    Ryu, W.S.2
  • 40
    • 79960911333 scopus 로고    scopus 로고
    • The physical and functional thermal sensitivity of bacterial chemoreceptors
    • Frank, V.; Koler, M.; Furst, S.; Vaknin, A. The physical and functional thermal sensitivity of bacterial chemoreceptors. J. Mol. Biol. 2011, 411, 554-566.
    • (2011) J. Mol. Biol , vol.411 , pp. 554-566
    • Frank, V.1    Koler, M.2    Furst, S.3    Vaknin, A.4
  • 41
    • 0030992385 scopus 로고    scopus 로고
    • Molecular architecture of bacterial flagellum
    • Namba, K.; Vonderviszt, F. Molecular architecture of bacterial flagellum. Q. Rev. Biophys. 1997, 30, 1-65.
    • (1997) Q. Rev. Biophys , vol.30 , pp. 1-65
    • Namba, K.1    Vonderviszt, F.2
  • 43
    • 0041673353 scopus 로고    scopus 로고
    • The rotary motor of bacterial flagella
    • Berg, H.C. The rotary motor of bacterial flagella. Annu. Rev. Biochem. 2003, 72, 19-54.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 19-54
    • Berg, H.C.1
  • 44
    • 1842588296 scopus 로고    scopus 로고
    • The bacterial flagellar motor: Structure and function of a complex molecular machine
    • Kojima, S.; Blair, D.F. The bacterial flagellar motor: structure and function of a complex molecular machine. Int. Rev. Cytol. 2004, 233, 93-134.
    • (2004) Int. Rev. Cytol , vol.233 , pp. 93-134
    • Kojima, S.1    Blair, D.F.2
  • 46
    • 52649147435 scopus 로고    scopus 로고
    • Bacterial flagellar motor
    • Sowa, Y.; Berry, R.M. Bacterial flagellar motor. Q. Rev. Biophys. 2008, 41, 103-132.
    • (2008) Q. Rev. Biophys , vol.41 , pp. 103-132
    • Sowa, Y.1    Berry, R.M.2
  • 47
    • 57149114304 scopus 로고    scopus 로고
    • Flagellar motility in bacteria structure and function of flagellar motor
    • Terashima, H.; Kojima, S.; Homma, M. Flagellar motility in bacteria structure and function of flagellar motor. Int. Rev. Cell Mol. Biol. 2008, 270, 39-85.
    • (2008) Int. Rev. Cell Mol. Biol , vol.270 , pp. 39-85
    • Terashima, H.1    Kojima, S.2    Homma, M.3
  • 48
    • 0016351193 scopus 로고
    • Flagellar rotation and the mechanism of bacterial motility
    • Silverman, M.; Simon, M. Flagellar rotation and the mechanism of bacterial motility. Nature 1974, 249, 73-74.
    • (1974) Nature , vol.249 , pp. 73-74
    • Silverman, M.1    Simon, M.2
  • 49
    • 0015759728 scopus 로고
    • Loss of bacterial motility under pressure
    • Meganathan, R.; Marquis, R.E. Loss of bacterial motility under pressure. Nature 1973, 246, 525-527.
    • (1973) Nature , vol.246 , pp. 525-527
    • Meganathan, R.1    Marquis, R.E.2
  • 50
    • 54949088268 scopus 로고    scopus 로고
    • The deep-sea bacterium Photobacterium profundum SS9 utilizes separate flagellar systems for swimming and swarming under high-pressure conditions
    • Eloe, E.A.; Lauro, F.M.; Vogel, R.F.; Bartlett, D.H. The deep-sea bacterium Photobacterium profundum SS9 utilizes separate flagellar systems for swimming and swarming under high-pressure conditions. Appl. Environ. Microbiol. 2008, 74, 6298-6305.
    • (2008) Appl. Environ. Microbiol , vol.74 , pp. 6298-6305
    • Eloe, E.A.1    Lauro, F.M.2    Vogel, R.F.3    Bartlett, D.H.4
  • 51
  • 52
    • 78049309085 scopus 로고    scopus 로고
    • Evidence for symmetry in the elementary process of bidirectional torque generation by the bacterial flagellar motor
    • Nakamura, S.; Kami-ike, N.; Yokota, J.P.; Minamino, T.; Namba, K. Evidence for symmetry in the elementary process of bidirectional torque generation by the bacterial flagellar motor. Proc. Natl. Acad. Sci. USA 2010, 107, 17616-17620.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17616-17620
    • Nakamura, S.1    Kami-Ike, N.2    Yokota, J.P.3    Minamino, T.4    Namba, K.5
  • 54
    • 0019802774 scopus 로고
    • Flagellar Motors of Alkalophilic Bacillus Are Powered by an Electrochemical Potential Gradient of Na+
    • Hirota, N.; Kitada, M.; Imae, Y. Flagellar Motors of Alkalophilic Bacillus Are Powered by an Electrochemical Potential Gradient of Na+. FEBS Lett. 1981, 132, 278-280.
    • (1981) FEBS Lett , vol.132 , pp. 278-280
    • Hirota, N.1    Kitada, M.2    Imae, Y.3
  • 55
    • 0037432553 scopus 로고    scopus 로고
    • Torque-speed relationship of the Na+-driven flagellar motor of Vibrio alginolyticus
    • Sowa, Y.; Hotta, H.; Homma, M.; Ishijima, A. Torque-speed relationship of the Na+-driven flagellar motor of Vibrio alginolyticus. J. Mol. Biol. 2003, 327, 1043-1051.
    • (2003) J. Mol. Biol , vol.327 , pp. 1043-1051
    • Sowa, Y.1    Hotta, H.2    Homma, M.3    Ishijima, A.4
  • 56
    • 0034719374 scopus 로고    scopus 로고
    • Torque-generating units of the flagellar motor of Escherichia coli have a high duty ratio
    • Ryu, W.S.; Berry, R.M.; Berg, H.C. Torque-generating units of the flagellar motor of Escherichia coli have a high duty ratio. Nature 2000, 403, 444-447.
    • (2000) Nature , vol.403 , pp. 444-447
    • Ryu, W.S.1    Berry, R.M.2    Berg, H.C.3
  • 58
    • 0027318440 scopus 로고
    • Study of the torque of the bacterial flagellar motor using a rotating electric field
    • Iwazawa, J.; Imae, Y.; Kobayasi, S. Study of the torque of the bacterial flagellar motor using a rotating electric field. Biophys. J. 1993, 64, 925-933.
    • (1993) Biophys. J , vol.64 , pp. 925-933
    • Iwazawa, J.1    Imae, Y.2    Kobayasi, S.3
  • 59
    • 0023128224 scopus 로고
    • Rapid Rotation of Flagellar Bundles in Swimming Bacteria
    • Lowe, G.; Meister, M.; Berg, H.C. Rapid Rotation of Flagellar Bundles in Swimming Bacteria. Nature 1987, 325, 637-640.
    • (1987) Nature , vol.325 , pp. 637-640
    • Lowe, G.1    Meister, M.2    Berg, H.C.3
  • 60
    • 0034036156 scopus 로고    scopus 로고
    • Torque-speed relationship of the flagellar rotary motor of
    • Chen, X.; Berg, H.C. Torque-speed relationship of the flagellar rotary motor of Escherichia coli. Biophys. J. 2000, 78, 1036-1041.
    • (2000) Escherichia Coli. Biophys. J , vol.78 , pp. 1036-1041
    • Chen, X.1    Berg, H.C.2
  • 61
    • 77952765661 scopus 로고    scopus 로고
    • Thermal and solvent-isotope effects on the flagellar rotary motor near zero load
    • Yuan, J.; Berg, H.C. Thermal and solvent-isotope effects on the flagellar rotary motor near zero load. Biophys. J. 2010, 98, 2121-2126.
    • (2010) Biophys. J , vol.98 , pp. 2121-2126
    • Yuan, J.1    Berg, H.C.2
  • 62
    • 79956150233 scopus 로고    scopus 로고
    • Two methods of temperature control for single-molecule measurements
    • Baker, M.A.; Inoue, Y.; Takeda, K.; Ishijima, A.; Berry, R.M. Two methods of temperature control for single-molecule measurements. Eur. Biophys. J. 2011, 40, 651-660.
    • (2011) Eur. Biophys. J , vol.40 , pp. 651-660
    • Baker, M.A.1    Inoue, Y.2    Takeda, K.3    Ishijima, A.4    Berry, R.M.5
  • 63
    • 0018944914 scopus 로고
    • Energetics of Flagellar Rotation in Bacteria
    • Manson, M.D.; Tedesco, P.M.; Berg, H.C. Energetics of Flagellar Rotation in Bacteria. J. Mol. Biol. 1980, 138, 541-561.
    • (1980) J. Mol. Biol , vol.138 , pp. 541-561
    • Manson, M.D.1    Tedesco, P.M.2    Berg, H.C.3
  • 64
    • 0019215039 scopus 로고
    • Quantitative measurements of proton motive force and motility in Bacillus subtilis
    • Shioi, J.I.; Matsuura, S.; Imae, Y. Quantitative measurements of proton motive force and motility in Bacillus subtilis. J. Bacteriol. 1980, 144, 891-897.
    • (1980) J. Bacteriol , vol.144 , pp. 891-897
    • Shioi, J.I.1    Matsuura, S.2    Imae, Y.3
  • 65
    • 0025058346 scopus 로고
    • The MotA Protein of Escherichia-coli is a proton-conducting component of the flagellar motor
    • Blair, D.F.; Berg, H.C. The MotA Protein of Escherichia-coli is a proton-conducting component of the flagellar motor. Cell 1990, 60, 439-449.
    • (1990) Cell , vol.60 , pp. 439-449
    • Blair, D.F.1    Berg, H.C.2
  • 66
    • 0347357933 scopus 로고    scopus 로고
    • Solubilization and purification of the MotA/MotB complex of Escherichia coli
    • Kojima, S.; Blair, D.F. Solubilization and purification of the MotA/MotB complex of Escherichia coli. Biochemistry 2004, 43, 26-34.
    • (2004) Biochemistry , vol.43 , pp. 26-34
    • Kojima, S.1    Blair, D.F.2
  • 67
    • 0346727448 scopus 로고    scopus 로고
    • Arrangement of core membrane segments in the MotA/MotB proton-channel complex of Escherichia coli
    • Braun, T.F.; Al-Mawsawi, L.Q.; Kojima, S.; Blair, D.F. Arrangement of core membrane segments in the MotA/MotB proton-channel complex of Escherichia coli. Biochemistry 2004, 43, 35-45.
    • (2004) Biochemistry , vol.43 , pp. 35-45
    • Braun, T.F.1    Al-Mawsawi, L.Q.2    Kojima, S.3    Blair, D.F.4
  • 68
    • 48149085753 scopus 로고    scopus 로고
    • Clusters of charged residues at the C terminus of MotA and N terminus of MotB are important for function of the Escherichia coli flagellar motor
    • Hosking, E.R.; Manson, M.D. Clusters of charged residues at the C terminus of MotA and N terminus of MotB are important for function of the Escherichia coli flagellar motor. J. Bacteriol. 2008, 190, 5517-5521.
    • (2008) J. Bacteriol , vol.190 , pp. 5517-5521
    • Hosking, E.R.1    Manson, M.D.2
  • 69
    • 1442326719 scopus 로고    scopus 로고
    • Structure of the rotor of the bacterial flagellar motor revealed by electron cryomicroscopy and single-particle image analysis
    • Suzuki, H.; Yonekura, K.; Namba, K. Structure of the rotor of the bacterial flagellar motor revealed by electron cryomicroscopy and single-particle image analysis. J. Mol. Biol. 2004, 337, 105-113.
    • (2004) J. Mol. Biol , vol.337 , pp. 105-113
    • Suzuki, H.1    Yonekura, K.2    Namba, K.3
  • 70
    • 77955924240 scopus 로고    scopus 로고
    • Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching
    • Lee, L.K.; Ginsburg, M.A.; Crovace, C.; Donohoe, M.; Stock, D. Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching. Nature 2010, 466, 996-1000.
    • (2010) Nature , vol.466 , pp. 996-1000
    • Lee, L.K.1    Ginsburg, M.A.2    Crovace, C.3    Donohoe, M.4    Stock, D.5
  • 71
    • 79958063382 scopus 로고    scopus 로고
    • Structural insight into the rotational switching mechanism of the bacterial flagellar motor
    • Minamino, T.; Imada, K.; Kinoshita, M.; Nakamura, S.; Morimoto, Y.V.; Namba, K. Structural insight into the rotational switching mechanism of the bacterial flagellar motor. PLoS Biol. 2011, 9, e1000616.
    • (2011) PLoS Biol , vol.9
    • Minamino, T.1    Imada, K.2    Kinoshita, M.3    Nakamura, S.4    Morimoto, Y.V.5    Namba, K.6
  • 73
    • 0032568636 scopus 로고    scopus 로고
    • Electrostatic interactions between rotor and stator in the bacterial flagellar motor
    • Zhou, J.; Lloyd, S.A.; Blair, D.F. Electrostatic interactions between rotor and stator in the bacterial flagellar motor. Proc. Natl. Acad. Sci. USA 1998, 95, 6436-6441.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6436-6441
    • Zhou, J.1    Lloyd, S.A.2    Blair, D.F.3
  • 74
    • 0031557399 scopus 로고    scopus 로고
    • Charged residues of the rotor protein FliG essential for torque generation in the flagellar motor of Escherichia coli
    • Lloyd, S.A.; Blair, D.F. Charged residues of the rotor protein FliG essential for torque generation in the flagellar motor of Escherichia coli. J. Mol. Biol. 1997, 266, 733-744.
    • (1997) J. Mol. Biol , vol.266 , pp. 733-744
    • Lloyd, S.A.1    Blair, D.F.2
  • 75
    • 0035980267 scopus 로고    scopus 로고
    • Conformational change in the stator of the bacterial flagellar motor
    • Kojima, S.; Blair, D.F. Conformational change in the stator of the bacterial flagellar motor. Biochemistry 2001, 40, 13041-13050.
    • (2001) Biochemistry , vol.40 , pp. 13041-13050
    • Kojima, S.1    Blair, D.F.2
  • 76
    • 53849145309 scopus 로고    scopus 로고
    • Suppressor analysis of the MotB(D33E) mutation to probe bacterial flagellar motor dynamics coupled with proton translocation
    • Che, Y.S.; Nakamura, S.; Kojima, S.; Kami-ike, N.; Namba, K.; Minamino, T. Suppressor analysis of the MotB(D33E) mutation to probe bacterial flagellar motor dynamics coupled with proton translocation. J. Bacteriol. 2008, 190, 6660-6667.
    • (2008) J. Bacteriol , vol.190 , pp. 6660-6667
    • Che, Y.S.1    Nakamura, S.2    Kojima, S.3    Kami-Ike, N.4    Namba, K.5    Minamino, T.6
  • 77
    • 59149087248 scopus 로고    scopus 로고
    • Effect of intracellular pH on the torque-speed relationship of bacterial proton-driven flagellar motor
    • Nakamura, S.; Kami-ike, N.; Yokota, J.P.; Kudo, S.; Minamino, T.; Namba, K. Effect of intracellular pH on the torque-speed relationship of bacterial proton-driven flagellar motor. J. Mol. Biol. 2009, 386, 332-338.
    • (2009) J. Mol. Biol , vol.386 , pp. 332-338
    • Nakamura, S.1    Kami-Ike, N.2    Yokota, J.P.3    Kudo, S.4    Minamino, T.5    Namba, K.6
  • 78
    • 0025148428 scopus 로고
    • Abrupt changes in flagellar rotation observed by laser dark-field microscopy
    • Kudo, S.; Magariyama, Y.; Aizawa, S. Abrupt changes in flagellar rotation observed by laser dark-field microscopy. Nature 1990, 346, 677-680.
    • (1990) Nature , vol.346 , pp. 677-680
    • Kudo, S.1    Magariyama, Y.2    Aizawa, S.3
  • 79
    • 78650273375 scopus 로고    scopus 로고
    • A simple backscattering microscope for fast tracking of biological molecules
    • Sowa, Y.; Steel, B.C.; Berry, R.M. A simple backscattering microscope for fast tracking of biological molecules. Rev. Sci. Instrum. 2010, 81, 113704.
    • (2010) Rev. Sci. Instrum , vol.81 , pp. 113704
    • Sowa, Y.1    Steel, B.C.2    Berry, R.M.3
  • 80
    • 76249126819 scopus 로고    scopus 로고
    • Conformational spread as a mechanism for cooperativity in the bacterial flagellar switch
    • Bai, F.; Branch, R.W.; Nicolau, D.V., Jr.; Pilizota, T.; Steel, B.C.; Maini, P.K.; Berry, R.M. Conformational spread as a mechanism for cooperativity in the bacterial flagellar switch. Science 2010, 327, 685-689.
    • (2010) Science , vol.327 , pp. 685-689
    • Bai, F.1    Branch, R.W.2    Nicolau Jr., D.V.3    Pilizota, T.4    Steel, B.C.5    Maini, P.K.6    Berry, R.M.7
  • 85
    • 84859832789 scopus 로고    scopus 로고
    • Functioning nanomachines seen in real-time in living bacteria using single-molecule and super-resolution fluorescence imaging
    • Chiu, S.W.; Leake, M.C. Functioning nanomachines seen in real-time in living bacteria using single-molecule and super-resolution fluorescence imaging. Int. J. Mol. Sci. 2011, 12, 2518-2542.
    • (2011) Int. J. Mol. Sci , vol.12 , pp. 2518-2542
    • Chiu, S.W.1    Leake, M.C.2
  • 86
    • 77955102352 scopus 로고    scopus 로고
    • Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells
    • Taniguchi, Y.; Choi, P.J.; Li, G.W.; Chen, H.; Babu, M.; Hearn, J.; Emili, A.; Xie, X.S. Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells. Science 2010, 329, 533-538.
    • (2010) Science , vol.329 , pp. 533-538
    • Taniguchi, Y.1    Choi, P.J.2    Li, G.W.3    Chen, H.4    Babu, M.5    Hearn, J.6    Emili, A.7    Xie, X.S.8
  • 87
    • 84863229704 scopus 로고    scopus 로고
    • Helical insertion of peptidoglycan produces chiral ordering of the bacterial cell wall
    • Wang, S.; Furchtgott, L.; Huang, K.C.; Shaevitz, J.W. Helical insertion of peptidoglycan produces chiral ordering of the bacterial cell wall. Proc. Natl. Acad. Sci. USA 2012, 109, E595-E604.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109
    • Wang, S.1    Furchtgott, L.2    Huang, K.C.3    Shaevitz, J.W.4
  • 88
    • 0018189924 scopus 로고
    • Complementation analysis and deletion mapping of Escherichia coli mutants defective in chemotaxis
    • Parkinson, J.S. Complementation analysis and deletion mapping of Escherichia coli mutants defective in chemotaxis. J. Bacteriol. 1978, 135, 45-53.
    • (1978) J. Bacteriol , vol.135 , pp. 45-53
    • Parkinson, J.S.1
  • 90
    • 79960385568 scopus 로고    scopus 로고
    • Characterization of the periplasmic region of PomB, a Na+-driven flagellar stator protein in Vibrio alginolyticus
    • Li, N.; Kojima, S.; Homma, M. Characterization of the periplasmic region of PomB, a Na+-driven flagellar stator protein in Vibrio alginolyticus. J. Bacteriol. 2011, 193, 3773-3784.
    • (2011) J. Bacteriol , vol.193 , pp. 3773-3784
    • Li, N.1    Kojima, S.2    Homma, M.3
  • 91
    • 0031683635 scopus 로고    scopus 로고
    • Deletion analysis of MotA and MotB, components of the force-generating unit in the flagellar motor of Salmonella
    • Muramoto, K.; Macnab, R.M. Deletion analysis of MotA and MotB, components of the force-generating unit in the flagellar motor of Salmonella. Mol. Microbiol. 1998, 29, 1191-1202.
    • (1998) Mol. Microbiol , vol.29 , pp. 1191-1202
    • Muramoto, K.1    Macnab, R.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.