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Volumn 53, Issue 24, 2014, Pages 4072-4080

ATP-induced dimerization of the F0F1 ε subunit from bacillus PS3: A hydrogen exchange-mass spectrometry study

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOLOGY; CIRCULAR DICHROISM SPECTROSCOPY; DIMERIZATION; HYDROLYSIS; MASS SPECTROMETRY; STABILIZATION;

EID: 84903162053     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5004684     Document Type: Article
Times cited : (5)

References (61)
  • 1
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • Boyer, P. D. (1997) The ATP synthase-a splendid molecular machine Annu. Rev. Biochem. 66, 717-749
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 2
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock, D., Leslie, A. G. W., and Walker, J. E. (1999) Molecular architecture of the rotary motor in ATP synthase Science 286, 1700-1705
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 4
    • 84879967659 scopus 로고    scopus 로고
    • Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation
    • Schmidt, C., Zhou, M., Marriot, H., Morgner, N., Politis, A., and Robinson, C. V. (2013) Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation Nat. Commun. 4, 1-11
    • (2013) Nat. Commun. , vol.4 , pp. 1-11
    • Schmidt, C.1    Zhou, M.2    Marriot, H.3    Morgner, N.4    Politis, A.5    Robinson, C.V.6
  • 7
    • 24944464164 scopus 로고    scopus 로고
    • 1-ATP synthase: The conformation of subunit ε might e determined by directionality of subunit γ rotation
    • 1-ATP synthase: the conformation of subunit ε might e determined by directionality of subunit γ rotation FEBS Lett. 579, 5114-5118
    • (2005) FEBS Lett. , vol.579 , pp. 5114-5118
    • Feniouk, B.A.1    Junge, W.2
  • 8
    • 76249120489 scopus 로고    scopus 로고
    • Conformational transitions of subunit ε in ATP synthase from thermophilic Bacillus PS3
    • Feniouk, B. A., Kato-Yamada, Y., Yoshida, M., and Suzuki, T. (2010) Conformational transitions of subunit ε in ATP synthase from thermophilic Bacillus PS3 Biophys. J. 98, 434-442
    • (2010) Biophys. J. , vol.98 , pp. 434-442
    • Feniouk, B.A.1    Kato-Yamada, Y.2    Yoshida, M.3    Suzuki, T.4
  • 9
    • 84875967309 scopus 로고    scopus 로고
    • The ε-inhibited state forms after ATP hydrolysis, is distinct fom the ADP-inhibited state, and responds dnamically to catalytic site ligands
    • Shah, N. B., Hutcheon, M. L., Haarer, B. K., and Duncan, T. M. (2013) The ε-inhibited state forms after ATP hydrolysis, is distinct fom the ADP-inhibited state, and responds dnamically to catalytic site ligands J. Biol. Chem. 288, 9383-9395
    • (2013) J. Biol. Chem. , vol.288 , pp. 9383-9395
    • Shah, N.B.1    Hutcheon, M.L.2    Haarer, B.K.3    Duncan, T.M.4
  • 11
    • 77951214694 scopus 로고    scopus 로고
    • Activation and stiffness of the inhibited states of F-1-ATPase probed by single-molecule manipulation
    • Saita, E., Iino, R., Suzuki, T., Feniouk, B. A., Kinosita, K., and Yoshida, M. (2010) Activation and stiffness of the inhibited states of F-1-ATPase probed by single-molecule manipulation J. Biol. Chem. 285, 11411-11417
    • (2010) J. Biol. Chem. , vol.285 , pp. 11411-11417
    • Saita, E.1    Iino, R.2    Suzuki, T.3    Feniouk, B.A.4    Kinosita, K.5    Yoshida, M.6
  • 13
    • 0032584582 scopus 로고    scopus 로고
    • Direct observation of the rotation of epsilon subunit in F-1-ATPase
    • Kato-Yamada, Y., Noji, H., Yasuda, R., Kinosita, K., and Yoshida, M. (1998) Direct observation of the rotation of epsilon subunit in F-1-ATPase J. Biol. Chem. 273, 19375-19377
    • (1998) J. Biol. Chem. , vol.273 , pp. 19375-19377
    • Kato-Yamada, Y.1    Noji, H.2    Yasuda, R.3    Kinosita, K.4    Yoshida, M.5
  • 14
  • 15
    • 33644866074 scopus 로고    scopus 로고
    • The role of the ε subunit in the Escherichia coli ATP Synthase: The C-terminal domain is required for efficient energy coupling
    • Cipriano, D. J. and Dunn, S. D. (2006) The role of the ε subunit in the Escherichia coli ATP Synthase: the C-terminal domain is required for efficient energy coupling J. Biol. Chem. 281, 501-507
    • (2006) J. Biol. Chem. , vol.281 , pp. 501-507
    • Cipriano, D.J.1    Dunn, S.D.2
  • 16
    • 0018908352 scopus 로고
    • Characterization of the inhibitory (epsilon) subunit of the proton-translocating adenosine triphosphatase from Escherichia coli
    • Sternweis, P. C. and Smith, J. B. (1980) Characterization of the inhibitory (epsilon) subunit of the proton-translocating adenosine triphosphatase from Escherichia coli Biochemistry 19, 526-531
    • (1980) Biochemistry , vol.19 , pp. 526-531
    • Sternweis, P.C.1    Smith, J.B.2
  • 17
    • 0025323480 scopus 로고
    • Activation of Escherichia coli F1 ATPase by lauryldimethylamine oxide and ethylene glycol: Relationship of ATPase activity to the interaction of the epsilon and beta subunits
    • Dunn, S. D., Tozer, R. G., and Zadorozny, V. D. (1990) Activation of Escherichia coli F1 ATPase by lauryldimethylamine oxide and ethylene glycol: relationship of ATPase activity to the interaction of the epsilon and beta subunits Biochemistry 29, 4335-4340
    • (1990) Biochemistry , vol.29 , pp. 4335-4340
    • Dunn, S.D.1    Tozer, R.G.2    Zadorozny, V.D.3
  • 18
    • 0030611634 scopus 로고    scopus 로고
    • Crystal structure of the ε subunit of the proton-translocating ATP synthase from Escherichia coli
    • Uhlin, U., Cox, G. B., and Guss, J. M. (1997) Crystal structure of the ε subunit of the proton-translocating ATP synthase from Escherichia coli Structure 5, 1219-1230
    • (1997) Structure , vol.5 , pp. 1219-1230
    • Uhlin, U.1    Cox, G.B.2    Guss, J.M.3
  • 19
    • 0032500380 scopus 로고    scopus 로고
    • Solution structure of the epsilon subunit of the F-1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex
    • Wilkens, S. and Capaldi, R. A. (1998) Solution structure of the epsilon subunit of the F-1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex J. Biol. Chem. 273, 26645-26651
    • (1998) J. Biol. Chem. , vol.273 , pp. 26645-26651
    • Wilkens, S.1    Capaldi, R.A.2
  • 20
    • 0033766435 scopus 로고    scopus 로고
    • The structure of the central stalk in bovine F-1-ATPase at 2.4 angstrom resolution
    • Gibbons, C., Montgomery, M. G., Leslie, A. G. W., and Walker, J. E. (2000) The structure of the central stalk in bovine F-1-ATPase at 2.4 angstrom resolution Nat. Struct. Biol. 7, 1055-1061
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1055-1061
    • Gibbons, C.1    Montgomery, M.G.2    Leslie, A.G.W.3    Walker, J.E.4
  • 21
    • 0026656847 scopus 로고
    • Determination of the 1-ethyl-3-(3-dimethylamino)propyl-carbodiimide- induced cross-link between the beta and epsilon subunits of Escherichia coli F1-ATPase
    • Dallmann, H. G., Flynn, T. G., and Dunn, S. D. (1992) Determination of the 1-ethyl-3-(3-dimethylamino)propyl-carbodiimide-induced cross-link between the beta and epsilon subunits of Escherichia coli F1-ATPase J. Biol. Chem. 267, 18953-18960
    • (1992) J. Biol. Chem. , vol.267 , pp. 18953-18960
    • Dallmann, H.G.1    Flynn, T.G.2    Dunn, S.D.3
  • 22
    • 0033623349 scopus 로고    scopus 로고
    • Structure of the gamma-epsilon complex of ATP synthase
    • Rodgers, A. J. W. and Wilce, M. C. J. (2000) Structure of the gamma-epsilon complex of ATP synthase Nat. Struct. Biol. 7, 1051-1054
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1051-1054
    • Rodgers, A.J.W.1    Wilce, M.C.J.2
  • 25
    • 0345306622 scopus 로고    scopus 로고
    • 1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of ε subunit in response to proton motive force and ADP/ATP balance
    • 1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of ε subunit in response to proton motive force and ADP/ATP balance J. Biol. Chem. 278, 46840-46846
    • (2003) J. Biol. Chem. , vol.278 , pp. 46840-46846
    • Suzuki, A.1    Murakami, K.2    Lino, R.3    Suzuki, J.4    Ono, S.5    Shirakihara, Y.6    Yoshida, M.7
  • 29
    • 28844477927 scopus 로고    scopus 로고
    • 1-ATPase binds ATP
    • 1-ATPase binds ATP FEBS Lett. 579, 6875-6878
    • (2005) FEBS Lett. , vol.579 , pp. 6875-6878
    • Kato-Yamada, Y.1
  • 33
    • 79951887389 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for studying protein structure and dynamics
    • Konermann, L., Pan, J., and Liu, Y. (2011) Hydrogen exchange mass spectrometry for studying protein structure and dynamics Chem. Soc. Rev. 40, 1224-1234
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 1224-1234
    • Konermann, L.1    Pan, J.2    Liu, Y.3
  • 34
    • 84878285699 scopus 로고    scopus 로고
    • Mass spectrometry-based methods to study protein architecture and dynamics
    • Kaltashov, I. A., Bobst, C. E., and Abzalimov, R. R. (2013) Mass spectrometry-based methods to study protein architecture and dynamics Protein Sci. 22, 530-544
    • (2013) Protein Sci. , vol.22 , pp. 530-544
    • Kaltashov, I.A.1    Bobst, C.E.2    Abzalimov, R.R.3
  • 35
    • 84863207545 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry: Are we out of the quicksand?
    • Iacob, R. E. and Engen, J. R. (2012) Hydrogen exchange mass spectrometry: are we out of the quicksand? J. Am. Soc. Mass Spectrom. 23, 1003-1010
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 1003-1010
    • Iacob, R.E.1    Engen, J.R.2
  • 36
    • 33750320427 scopus 로고    scopus 로고
    • Hydrogen exchange and mass spectrometry: A historical perspective
    • Englander, S. W. (2006) Hydrogen exchange and mass spectrometry: a historical perspective J. Am. Soc. Mass Spectrom. 17, 1481-1489
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1481-1489
    • Englander, S.W.1
  • 37
    • 84859904015 scopus 로고    scopus 로고
    • Measuring dynamics in weakly structured regions of proteins using microfluidics-enabled subsecond H/D exchange mass spectrometry
    • Rob, T., Liuni, P., Gill, P. K., Zhu, S. L., Balachandran, N., Berti, P. J., and Wilson, D. J. (2012) Measuring dynamics in weakly structured regions of proteins using microfluidics-enabled subsecond H/D exchange mass spectrometry Anal. Chem. 84, 3771-3779
    • (2012) Anal. Chem. , vol.84 , pp. 3771-3779
    • Rob, T.1    Liuni, P.2    Gill, P.K.3    Zhu, S.L.4    Balachandran, N.5    Berti, P.J.6    Wilson, D.J.7
  • 38
    • 0028609035 scopus 로고
    • Mass spectrometric measurement of protein amide hydrogen exchange rates of apo- and holo-myoglobin
    • Johnson, R. S. and Walsh, K. A. (1994) Mass spectrometric measurement of protein amide hydrogen exchange rates of apo- and holo-myoglobin Protein Sci. 3, 2411-2418
    • (1994) Protein Sci. , vol.3 , pp. 2411-2418
    • Johnson, R.S.1    Walsh, K.A.2
  • 39
    • 0037019523 scopus 로고    scopus 로고
    • A general mass spectrometry-based assay for the quantitation of protein-ligand binding interactions in solution
    • Powell, K. D., Ghaemmaghami, S., Wang, M. Z., Ma, L., Oas, T. G., and Fitzgerald, M. C. (2002) A general mass spectrometry-based assay for the quantitation of protein-ligand binding interactions in solution J. Am. Chem. Soc. 124, 10256-10257
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10256-10257
    • Powell, K.D.1    Ghaemmaghami, S.2    Wang, M.Z.3    Ma, L.4    Oas, T.G.5    Fitzgerald, M.C.6
  • 40
    • 0038293125 scopus 로고    scopus 로고
    • Quantification of protein-ligand interactions by mass spectrometry, titration, and H/D exchange: PLIMSTEX
    • Zhu, M. M., Rempel, D. L., Du, Z. H., and Gross, M. L. (2003) Quantification of protein-ligand interactions by mass spectrometry, titration, and H/D exchange: PLIMSTEX J. Am. Chem. Soc. 125, 5252-5253
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5252-5253
    • Zhu, M.M.1    Rempel, D.L.2    Du, Z.H.3    Gross, M.L.4
  • 41
    • 84866103277 scopus 로고    scopus 로고
    • Dissection of porphyrin-induced conformational dynamics in the heme biosynthesis enzyme ferrochelatase
    • Asuru, A. P., An, M., and Busenlehner, L. S. (2012) Dissection of porphyrin-induced conformational dynamics in the heme biosynthesis enzyme ferrochelatase Biochemistry 51, 7116-7127
    • (2012) Biochemistry , vol.51 , pp. 7116-7127
    • Asuru, A.P.1    An, M.2    Busenlehner, L.S.3
  • 42
    • 80053581731 scopus 로고    scopus 로고
    • Mapping unstructured regions and synergistic folding in intrinsically disordered proteins with amide H/D exchange mass spectrometry
    • Keppel, T. R., Howard, B. A., and Weis, D. D. (2011) Mapping unstructured regions and synergistic folding in intrinsically disordered proteins with amide H/D exchange mass spectrometry Biochemistry 50, 8722-8732
    • (2011) Biochemistry , vol.50 , pp. 8722-8732
    • Keppel, T.R.1    Howard, B.A.2    Weis, D.D.3
  • 44
    • 84858277365 scopus 로고    scopus 로고
    • Probing protein interactions with hydrogen/deuterium exchange and mass spectrometry - A review
    • Percy, A. J., Rey, M., Burns, K. M., and Schriemer, D. C. (2012) Probing protein interactions with hydrogen/deuterium exchange and mass spectrometry-a review Anal. Chim. Acta 721, 7-21
    • (2012) Anal. Chim. Acta , vol.721 , pp. 7-21
    • Percy, A.J.1    Rey, M.2    Burns, K.M.3    Schriemer, D.C.4
  • 45
    • 79951907062 scopus 로고    scopus 로고
    • Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactions
    • Chalmers, M. J., Busby, S. A., Pascal, B. D., West, G. M., and Griffin, P. R. (2011) Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactions Exp. Rev. Proteomics 8, 43-59
    • (2011) Exp. Rev. Proteomics , vol.8 , pp. 43-59
    • Chalmers, M.J.1    Busby, S.A.2    Pascal, B.D.3    West, G.M.4    Griffin, P.R.5
  • 46
    • 0027179864 scopus 로고
    • Location of conserved residue histidine-38 of the ε subunit of Escherichia coli ATP synthase
    • Skakoon, E. N. and Dunn, S. D. (1993) Location of conserved residue histidine-38 of the ε subunit of Escherichia coli ATP synthase Arch. Biochem. Biophys. 302, 272-278
    • (1993) Arch. Biochem. Biophys. , vol.302 , pp. 272-278
    • Skakoon, E.N.1    Dunn, S.D.2
  • 47
    • 0037053396 scopus 로고    scopus 로고
    • Genetic fusions of globular proteins to the ε subunit of the Escherichia coli ATP synthase
    • Cipriano, D. J. and Dunn, S. D. (2002) Genetic fusions of globular proteins to the ε subunit of the Escherichia coli ATP synthase J. Biol. Chem. 277, 16782-16790
    • (2002) J. Biol. Chem. , vol.277 , pp. 16782-16790
    • Cipriano, D.J.1    Dunn, S.D.2
  • 49
    • 0034009520 scopus 로고    scopus 로고
    • Size-distrubution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. (2000) Size-distrubution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling Biophys. J. 3, 1606-1619
    • (2000) Biophys. J. , vol.3 , pp. 1606-1619
    • Schuck, P.1
  • 50
    • 0036154258 scopus 로고    scopus 로고
    • Size-distrubution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • Schuck, P., Perugini, M. A., Gonzales, N. R., Howlett, G. J., and Schubert, D. (2002) Size-distrubution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems Biophys. J. 82, 1096-1111
    • (2002) Biophys. J. , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 51
    • 23444456924 scopus 로고    scopus 로고
    • How to study protein by circular dichroism
    • Kelly, S. W., Jess, T. J., and Price, N. C. (2005) How to study protein by circular dichroism Biochim. Biophys. Acta 1751, 119-139
    • (2005) Biochim. Biophys. Acta , vol.1751 , pp. 119-139
    • Kelly, S.W.1    Jess, T.J.2    Price, N.C.3
  • 52
    • 1542319732 scopus 로고    scopus 로고
    • Relationship between growth rate and ATP concentration in Escherichia col i - A bioassay for available cellular ATP
    • Schneider, D. A. and Gourse, R. L. (2004) Relationship between growth rate and ATP concentration in Escherichia col i-a bioassay for available cellular ATP J. Biol. Chem. 279, 8262-8268
    • (2004) J. Biol. Chem. , vol.279 , pp. 8262-8268
    • Schneider, D.A.1    Gourse, R.L.2
  • 53
    • 3042709505 scopus 로고    scopus 로고
    • Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase
    • Liang, Z.-X., Lee, T., Resing, K. A., Ahn, N. G., and Klinman, J. P. (2004) Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase Proc. Natl. Acad. Sci. U.S.A. 101, 9556-9561
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 9556-9561
    • Liang, Z.-X.1    Lee, T.2    Resing, K.A.3    Ahn, N.G.4    Klinman, J.P.5
  • 55
    • 79955790484 scopus 로고    scopus 로고
    • Mapping the protein-protein interface between a toxin and its cognate antitoxin from the bacterial pathogen Streptococcus pyogenes
    • Sperry, J. B., Smith, C. L., Caparon, M. G., Ellenberger, T., and Gross, M. L. (2011) Mapping the protein-protein interface between a toxin and its cognate antitoxin from the bacterial pathogen Streptococcus pyogenes Biochemistry 50, 4038-4045
    • (2011) Biochemistry , vol.50 , pp. 4038-4045
    • Sperry, J.B.1    Smith, C.L.2    Caparon, M.G.3    Ellenberger, T.4    Gross, M.L.5
  • 56
    • 80054939273 scopus 로고    scopus 로고
    • Analysis of oligomeric stability of insulin analogs using hydrogen/deuterium exchange mass spectrometry
    • Nakazawa, S., Hashii, N., Harazono, A., and Kawasaki, N. (2012) Analysis of oligomeric stability of insulin analogs using hydrogen/deuterium exchange mass spectrometry Anal. Biochem. 420, 61-67
    • (2012) Anal. Biochem. , vol.420 , pp. 61-67
    • Nakazawa, S.1    Hashii, N.2    Harazono, A.3    Kawasaki, N.4
  • 57
    • 77952850206 scopus 로고    scopus 로고
    • SecA: A tale of two protomers
    • Sardis, M. F. and Economou, A. (2010) SecA: a tale of two protomers Mol. Microbiol. 76, 1070-1081
    • (2010) Mol. Microbiol. , vol.76 , pp. 1070-1081
    • Sardis, M.F.1    Economou, A.2
  • 58
    • 0030850230 scopus 로고    scopus 로고
    • Protein-protein crystal-packing contacts
    • Carugo, O. and Argos, P. (1997) Protein-protein crystal-packing contacts Protein Sci. 6, 2261-2263
    • (1997) Protein Sci. , vol.6 , pp. 2261-2263
    • Carugo, O.1    Argos, P.2
  • 60
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E. and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372, 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 61
    • 33748758703 scopus 로고    scopus 로고
    • γε sub-complex of thermophilic ATP synthase has the ability to bind ATP
    • Iizuka, S., Kato, S., Yoshida, M., and Kato-Yamada, Y. (2006) γε sub-complex of thermophilic ATP synthase has the ability to bind ATP Biochem. Biophys. Res. Commun. 349, 1368-1371
    • (2006) Biochem. Biophys. Res. Commun. , vol.349 , pp. 1368-1371
    • Iizuka, S.1    Kato, S.2    Yoshida, M.3    Kato-Yamada, Y.4


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