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Volumn 152, Issue 2, 2005, Pages 140-145

Purification, crystallization, and properties of F1-ATPase complexes from the thermoalkaliphilic Bacillus sp. strain TA2.A1

Author keywords

Crystallization; F1 ATPase; TA2.A1; Thermoalkaliphile; X ray

Indexed keywords

ADENOSINE TRIPHOSPHATE; METHYLAMINE; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SOLVENT;

EID: 27744598146     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2005.08.005     Document Type: Article
Times cited : (13)

References (30)
  • 1
    • 0028114231 scopus 로고
    • Structure at 2.8 a resolution of F1-ATPase from bovine heart mitochondria
    • J.P. Abrahams, A.G. Leslie, R. Lutter, and J.E. Walker Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria Nature 370 1994 621 628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 2
    • 0027207330 scopus 로고
    • Inherent asymmetry of the structure of F1-ATPase from bovine heart mitochondria at 6.5 a resolution
    • J.P. Abrahams, R. Lutter, R.J. Todd, M.J. van Raaij, A.G. Leslie, and J.E. Walker Inherent asymmetry of the structure of F1-ATPase from bovine heart mitochondria at 6.5 A resolution Embo. J. 12 1993 1775 1780
    • (1993) Embo. J. , vol.12 , pp. 1775-1780
    • Abrahams, J.P.1    Lutter, R.2    Todd, R.J.3    Van Raaij, M.J.4    Leslie, A.G.5    Walker, J.E.6
  • 3
    • 1542289939 scopus 로고    scopus 로고
    • Insights into the molecular mechanism of rotation in the Fo sector of ATP synthase
    • A. Aksimentiev, I.A. Balabin, R.H. Fillingame, and K. Schulten Insights into the molecular mechanism of rotation in the Fo sector of ATP synthase Biophys. J. 86 2004 1332 1344
    • (2004) Biophys. J. , vol.86 , pp. 1332-1344
    • Aksimentiev, A.1    Balabin, I.A.2    Fillingame, R.H.3    Schulten, K.4
  • 4
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase-some probabilities and possibilities
    • P.D. Boyer The binding change mechanism for ATP synthase-some probabilities and possibilities Biochim. Biophys. Acta 1140 1993 215 250
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 5
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase-a splendid molecular machine
    • P.D. Boyer The ATP synthase-a splendid molecular machine Annu. Rev. Biochem. 66 1997 717 749
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 6
    • 0037767525 scopus 로고    scopus 로고
    • Purification and biochemical characterization of the F1Fo-ATP synthase from thermoalkaliphilic Bacillus sp. strain TA2.A1
    • G.M. Cook, S. Keis, H.W. Morgan, C. von Ballmoos, U. Matthey, G. Kaim, and P. Dimroth Purification and biochemical characterization of the F1Fo-ATP synthase from thermoalkaliphilic Bacillus sp. strain TA2.A1 J. Bacteriol. 185 2003 4442 4449
    • (2003) J. Bacteriol. , vol.185 , pp. 4442-4449
    • Cook, G.M.1    Keis, S.2    Morgan, H.W.3    Von Ballmoos, C.4    Matthey, U.5    Kaim, G.6    Dimroth, P.7
  • 7
    • 0028790063 scopus 로고
    • Probing interactions of the Escherichia coli F0F1 ATP synthase beta and gamma subunits with disulphide cross-links
    • T.M. Duncan, Y. Zhou, V.V. Bulygin, M.L. Hutcheon, and R.L. Cross Probing interactions of the Escherichia coli F0F1 ATP synthase beta and gamma subunits with disulphide cross-links Biochem. Soc. Trans. 23 1995 736 741
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 736-741
    • Duncan, T.M.1    Zhou, Y.2    Bulygin, V.V.3    Hutcheon, M.L.4    Cross, R.L.5
  • 9
    • 0030611891 scopus 로고    scopus 로고
    • An improved purification of ECF1 and ECF1F0 by using a cytochrome bo-deficient strain of Escherichia coli facilitates crystallization of these complexes
    • G. Gruber, A. Hausrath, M. Sagermann, and R.A. Capaldi An improved purification of ECF1 and ECF1F0 by using a cytochrome bo-deficient strain of Escherichia coli facilitates crystallization of these complexes FEBS Lett. 410 1997 165 168
    • (1997) FEBS Lett. , vol.410 , pp. 165-168
    • Gruber, G.1    Hausrath, A.2    Sagermann, M.3    Capaldi, R.A.4
  • 10
    • 0026038362 scopus 로고
    • Plasmid transformation of Escherichia coli and other bacteria
    • D. Hanahan, J. Jessee, and F.R. Bloom Plasmid transformation of Escherichia coli and other bacteria Methods Enzymol. 204 1991 63 113
    • (1991) Methods Enzymol. , vol.204 , pp. 63-113
    • Hanahan, D.1    Jessee, J.2    Bloom, F.R.3
  • 11
    • 0035861587 scopus 로고    scopus 로고
    • The conformation of the epsilon- and gamma-subunits within the Escherichia coli F(1) ATPase
    • A.C. Hausrath, R.A. Capaldi, and B.W. Matthews The conformation of the epsilon- and gamma-subunits within the Escherichia coli F(1) ATPase J. Biol. Chem. 276 2001 47227 47232
    • (2001) J. Biol. Chem. , vol.276 , pp. 47227-47232
    • Hausrath, A.C.1    Capaldi, R.A.2    Matthews, B.W.3
  • 13
    • 0025196083 scopus 로고
    • Purification and reconstitution of the F1F0-ATP synthase from alkaliphilic Bacillus firmus OF4. Evidence that the enzyme translocates H+ but not Na+
    • D.B. Hicks, and T.A. Krulwich Purification and reconstitution of the F1F0-ATP synthase from alkaliphilic Bacillus firmus OF4. Evidence that the enzyme translocates H+ but not Na+ J. Biol. Chem. 265 1990 20547 20554
    • (1990) J. Biol. Chem. , vol.265 , pp. 20547-20554
    • Hicks, D.B.1    Krulwich, T.A.2
  • 14
    • 0025651603 scopus 로고
    • The ATPase of Bacillus alcalophilus. Purification and properties of the enzyme
    • A. Hoffmann, and P. Dimroth The ATPase of Bacillus alcalophilus. Purification and properties of the enzyme Eur. J. Biochem. 194 1990 423 430
    • (1990) Eur. J. Biochem. , vol.194 , pp. 423-430
    • Hoffmann, A.1    Dimroth, P.2
  • 15
    • 0025950163 scopus 로고
    • The electrochemical proton potential of Bacillus alcalophilus
    • A. Hoffmann, and P. Dimroth The electrochemical proton potential of Bacillus alcalophilus Eur. J. Biochem. 201 1991 467 473
    • (1991) Eur. J. Biochem. , vol.201 , pp. 467-473
    • Hoffmann, A.1    Dimroth, P.2
  • 16
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • w. Kabsch Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants J. Appl. Cryst. 26 1993 795 800
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 17
    • 1442287475 scopus 로고    scopus 로고
    • Cloning and molecular characterization of the atp operon encoding for the F1F0-ATP synthase from a thermoalkaliphilic Bacillus sp. strain TA2.A1
    • S. Keis, G. Kaim, P. Dimroth, and G.M. Cook Cloning and molecular characterization of the atp operon encoding for the F1F0-ATP synthase from a thermoalkaliphilic Bacillus sp. strain TA2.A1 Biochim. Biophys. Acta 1676 2004 112 117
    • (2004) Biochim. Biophys. Acta , vol.1676 , pp. 112-117
    • Keis, S.1    Kaim, G.2    Dimroth, P.3    Cook, G.M.4
  • 18
    • 0025376430 scopus 로고
    • Structure of the ATP synthase complex (ECF1F0) of Escherichia coli from cryoelectron microscopy
    • U. Lucken, E.P. Gogol, and R.A. Capaldi Structure of the ATP synthase complex (ECF1F0) of Escherichia coli from cryoelectron microscopy Biochemistry 29 1990 5339 5343
    • (1990) Biochemistry , vol.29 , pp. 5339-5343
    • Lucken, U.1    Gogol, E.P.2    Capaldi, R.A.3
  • 20
    • 17844367330 scopus 로고    scopus 로고
    • Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus
    • T. Meier, P. Polzer, K. Diederichs, W. Welte, and P. Dimroth Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus Science 308 2005 659 662
    • (2005) Science , vol.308 , pp. 659-662
    • Meier, T.1    Polzer, P.2    Diederichs, K.3    Welte, W.4    Dimroth, P.5
  • 21
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F1-ATPase
    • H. Noji, R. Yasuda, M. Yoshida, and K. Kinosita Jr. Direct observation of the rotation of F1-ATPase Nature 386 1997 299 302
    • (1997) Nature , vol.386 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita Jr., K.4
  • 22
    • 0037207875 scopus 로고    scopus 로고
    • Bioenergetic properties of the thermoalkaliphilic Bacillus sp. strain TA2.A1
    • K. Olsson, S. Keis, H.W. Morgan, P. Dimroth, and G.M. Cook Bioenergetic properties of the thermoalkaliphilic Bacillus sp. strain TA2.A1 J. Bacteriol. 185 2003 461 465
    • (2003) J. Bacteriol. , vol.185 , pp. 461-465
    • Olsson, K.1    Keis, S.2    Morgan, H.W.3    Dimroth, P.4    Cook, G.M.5
  • 23
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • V.K. Rastogi, and M.E. Girvin Structural changes linked to proton translocation by subunit c of the ATP synthase Nature 402 1999 263 268
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi, V.K.1    Girvin, M.E.2
  • 24
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F-ATPase
    • D. Sabbert, S. Engelbrecht, and W. Junge Intersubunit rotation in active F-ATPase Nature 381 1996 623 625
    • (1996) Nature , vol.381 , pp. 623-625
    • Sabbert, D.1    Engelbrecht, S.2    Junge, W.3
  • 25
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • H. Schagger, and G. von Jagow Tricine-sodium dodecyl sulfate- polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Anal. Biochem. 166 1987 368 379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 26
    • 0023839098 scopus 로고
    • ATP synthesis by oxidative phosphorylation
    • A.E. Senior ATP synthesis by oxidative phosphorylation Physiol. Rev. 68 1988 177 231
    • (1988) Physiol. Rev. , vol.68 , pp. 177-231
    • Senior, A.E.1
  • 28
    • 0038053885 scopus 로고    scopus 로고
    • ATP synthesis driven by proton transport in F1F0-ATP synthase
    • J. Weber, and A.E. Senior ATP synthesis driven by proton transport in F1F0-ATP synthase FEBS Lett. 545 2003 61 70
    • (2003) FEBS Lett. , vol.545 , pp. 61-70
    • Weber, J.1    Senior, A.E.2
  • 29
    • 0019882018 scopus 로고
    • Silver staining of proteins in polyacrylamide gels
    • W. Wray, T. Boulikas, V.P. Wray, and R. Hancock Silver staining of proteins in polyacrylamide gels Anal. Biochem. 118 1981 197 203
    • (1981) Anal. Biochem. , vol.118 , pp. 197-203
    • Wray, W.1    Boulikas, T.2    Wray, V.P.3    Hancock, R.4


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