메뉴 건너뛰기




Volumn 1817, Issue 10, 2012, Pages 1711-1721

Rotational catalysis in proton pumping ATPases: From E. coli F-ATPase to mammalian V-ATPase

Author keywords

ATP synthase; F ATPase; Single molecule observation; Subunit rotation; V ATPase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PROTON TRANSLOCATING ADENOSINE TRIPHOSPHATE SYNTHASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UNCLASSIFIED DRUG; VACUOLAR TYPE ADENOSINE TRIPHOSPHATE;

EID: 84864677023     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2012.03.015     Document Type: Conference Paper
Times cited : (50)

References (88)
  • 1
    • 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
  • 4
    • 0242657369 scopus 로고    scopus 로고
    • Mechanics of coupling proton movements to c-ring rotation in ATP synthase
    • R.H. Fillingame, C.M. Angevine, and O.Y. Dmitriev Mechanics of coupling proton movements to c-ring rotation in ATP synthase FEBS Lett. 555 2003 29 34
    • (2003) FEBS Lett. , vol.555 , pp. 29-34
    • Fillingame, R.H.1    Angevine, C.M.2    Dmitriev, O.Y.3
  • 5
    • 84954271321 scopus 로고    scopus 로고
    • Proton transporting ATPases: Introducing unique enzymes coupling catalysis and proton translocation through mechanical rotation
    • M. Futai, Y. Wada, J. Kaplan
    • M. Futai, G.H. Sun-Wada, and Y. Wada Proton transporting ATPases: introducing unique enzymes coupling catalysis and proton translocation through mechanical rotation M. Futai, Y. Wada, J. Kaplan, Handbook of ATPases: Biochemistry, Cell Biology, Pathophysiology 2004 237 260
    • (2004) Handbook of ATPases: Biochemistry, Cell Biology, Pathophysiology , pp. 237-260
    • Futai, M.1    Sun-Wada, G.H.2    Wada, Y.3
  • 7
    • 0018350899 scopus 로고
    • Specialized transducing phage λ carrying the genes for coupling factor of oxidative phosphorylation of Escherichia coli: Increased synthesis of coupling factor on induction of prophage λasn
    • H. Kanazawa, T. Miki, F. Tamura, T. Yura, and M. Futai Specialized transducing phage λ carrying the genes for coupling factor of oxidative phosphorylation of Escherichia coli: increased synthesis of coupling factor on induction of prophage λasn Proc. Natl. Acad. Sci. U. S. A. 76 1979 1126 1130
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 1126-1130
    • Kanazawa, H.1    Miki, T.2    Tamura, F.3    Yura, T.4    Futai, M.5
  • 8
    • 0024354291 scopus 로고
    • +-ATPase): Results by combined biochemical and molecular biological approaches
    • +-ATPase): results by combined biochemical and molecular biological approaches Annu. Rev. Biochem. 58 1989 111 136
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 111-136
    • Futai, M.1    Noumi, T.2    Maeda, M.3
  • 18
    • 0037109039 scopus 로고    scopus 로고
    • Subunit rotation of ATP synthase embedded in membranes: A or β subunit rotation relative to the c subunit ring
    • K. Nishio, A. Iwamoto-Kihara, A. Yamamoto, Y. Wada, and M. Futai Subunit rotation of ATP synthase embedded in membranes: a or β subunit rotation relative to the c subunit ring Proc. Natl. Acad. Sci. U. S. A. 99 2002 13448 13452
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 13448-13452
    • Nishio, K.1    Iwamoto-Kihara, A.2    Yamamoto, A.3    Wada, Y.4    Futai, M.5
  • 20
    • 3542998744 scopus 로고    scopus 로고
    • Diverse and essential roles of mammalian vacuolar-type proton pump ATPase: Toward the physiological understanding of inside acidic compartments
    • G.H. Sun-Wada, Y. Wada, and M. Futai Diverse and essential roles of mammalian vacuolar-type proton pump ATPase: toward the physiological understanding of inside acidic compartments Biochim. Biophys. Acta 1658 2004 106 114
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 106-114
    • Sun-Wada, G.H.1    Wada, Y.2    Futai, M.3
  • 21
    • 33644935227 scopus 로고    scopus 로고
    • + ATPase: Molecular structure and function, physiological roles and regulation
    • + ATPase: molecular structure and function, physiological roles and regulation J. Exp. Biol. 209 2006 577 589
    • (2006) J. Exp. Biol. , vol.209 , pp. 577-589
    • Beyenbach, K.W.1    Wieczorek, H.2
  • 22
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • M. Forgac Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology Nat. Rev. Mol. Cell Biol. 8 2007 917 929
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 917-929
    • Forgac, M.1
  • 23
    • 47349120492 scopus 로고    scopus 로고
    • +-ATPase in vesicular trafficking: Targeting, regulation and function
    • +-ATPase in vesicular trafficking: targeting, regulation and function Curr. Opin. Cell Biol. 20 2008 415 426
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 415-426
    • Marshansky, V.1    Futai, M.2
  • 24
    • 0038606551 scopus 로고    scopus 로고
    • Subunit rotation of vacuolar-type proton pumping ATPase: Relative rotation of the G and c subunits
    • T. Hirata, A. Iwamoto-Kihara, G.H. Sun-Wada, T. Okajima, Y. Wada, and M. Futai Subunit rotation of vacuolar-type proton pumping ATPase: relative rotation of the G and c subunits J. Biol. Chem. 278 2003 23714 23719
    • (2003) J. Biol. Chem. , vol.278 , pp. 23714-23719
    • Hirata, T.1    Iwamoto-Kihara, A.2    Sun-Wada, G.H.3    Okajima, T.4    Wada, Y.5    Futai, M.6
  • 28
    • 79961236945 scopus 로고    scopus 로고
    • High-speed atomic force microscopy reveals rotary catalysis of rotorless F-ATPase
    • T. Uchihashi, R. Iino, T. Ando, and H. Noji High-speed atomic force microscopy reveals rotary catalysis of rotorless F-ATPase Science 333 6043 2011 755 758
    • (2011) Science , vol.333 , Issue.6043 , pp. 755-758
    • Uchihashi, T.1    Iino, R.2    Ando, T.3    Noji, H.4
  • 31
    • 0028113029 scopus 로고
    • +-ATPase (ATP synthase) β subunit are essential for catalysis: Properties of 33 mutants between βglu-161 and βlys-201 residues
    • +-ATPase (ATP synthase) β subunit are essential for catalysis: properties of 33 mutants between βGlu-161 and βLys-201 residues J. Biochem. 116 1994 1139 1145
    • (1994) J. Biochem. , vol.116 , pp. 1139-1145
    • Park, M.Y.1    Omote, H.2    Maeda, M.3    Futai, M.4
  • 36
    • 0000240031 scopus 로고    scopus 로고
    • Escherichia coli ATP synthase α subunit Arg-376: The catalytic site arginine does not participate in the hydrolysis/synthesis reaction but is required for promotion to steady state
    • N.P. Le, H. Omote, Y. Wada, M.K. Al-Shawi, R.K. Nakamoto, and M. Futai Escherichia coli ATP synthase α subunit Arg-376: the catalytic site arginine does not participate in the hydrolysis/synthesis reaction but is required for promotion to steady state Biochemistry (Washington) 39 2000 2778 2783
    • (2000) Biochemistry (Washington) , vol.39 , pp. 2778-2783
    • Le, N.P.1    Omote, H.2    Wada, Y.3    Al-Shawi, M.K.4    Nakamoto, R.K.5    Futai, M.6
  • 39
    • 0030716497 scopus 로고    scopus 로고
    • Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue
    • K. Rittinger, P.A. Walker, J.F. Eccleston, S.J. Smerdon, and S.J. Gamblin Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue Nature 389 1997 758 762
    • (1997) Nature , vol.389 , pp. 758-762
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3    Smerdon, S.J.4    Gamblin, S.J.5
  • 43
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • D. Stock, A.G.W. Leslie, and J.E. Walker Molecular architecture of the rotary motor in ATP synthase Science 286 1999 1700 1705
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 44
    • 0035942281 scopus 로고    scopus 로고
    • The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10
    • W. Jiang, J. Hermolin, and R.H. Fillingame The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10 Proc. Natl. Acad. Sci. U. S. A. 98 2001 4966 4971
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 4966-4971
    • Jiang, W.1    Hermolin, J.2    Fillingame, R.H.3
  • 56
    • 0032547899 scopus 로고    scopus 로고
    • 1 motor of ATP synthase
    • 1 motor of ATP synthase Nature 396 1998 279 282
    • (1998) Nature , vol.396 , pp. 279-282
    • Wang, H.1    Oster, G.2
  • 58
    • 0025233785 scopus 로고
    • +-ATPase γ subunit of Escherichia coli. Role of the conserved carboxyl-terminal region
    • +-ATPase γ subunit of Escherichia coli. Role of the conserved carboxyl-terminal region J. Biol. Chem. 265 1990 5043 5048
    • (1990) J. Biol. Chem. , vol.265 , pp. 5043-5048
    • Iwamoto, A.1    Miki, J.2    Maeda, M.3    Futai, M.4
  • 59
    • 0026612451 scopus 로고
    • 1-ATPase γ subunit mutations perturb the coupling between catalysis and transport
    • 1-ATPase γ subunit mutations perturb the coupling between catalysis and transport J. Biol. Chem. 267 1992 20835 20839
    • (1992) J. Biol. Chem. , vol.267 , pp. 20835-20839
    • Shin, K.1    Nakamoto, R.K.2    Maeda, M.3    Futai, M.4
  • 60
    • 0027471965 scopus 로고
    • The γ subunit of the Escherichia coli ATP synthase. Mutations in the carboxyl-terminal region restore energy coupling to the amino-terminal mutant γmet-23 → Lys
    • R.K. Nakamoto, M. Maeda, and M. Futai The γ subunit of the Escherichia coli ATP synthase. Mutations in the carboxyl-terminal region restore energy coupling to the amino-terminal mutant γMet-23 → Lys J. Biol. Chem. 268 1993 867 872
    • (1993) J. Biol. Chem. , vol.268 , pp. 867-872
    • Nakamoto, R.K.1    Maeda, M.2    Futai, M.3
  • 61
    • 0029040551 scopus 로고
    • The ATP synthase γ subunit. Suppressor mutagenesis reveals three helical regions involved in energy coupling
    • R.K. Nakamoto, M.K. Al-Shawi, and M. Futai The ATP synthase γ subunit. Suppressor mutagenesis reveals three helical regions involved in energy coupling J. Biol. Chem. 270 1995 14042 14046
    • (1995) J. Biol. Chem. , vol.270 , pp. 14042-14046
    • Nakamoto, R.K.1    Al-Shawi, M.K.2    Futai, M.3
  • 62
    • 0030612021 scopus 로고    scopus 로고
    • i. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway
    • i. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway Biochemistry 36 1997 12961 12969
    • (1997) Biochemistry , vol.36 , pp. 12961-12969
    • Al-Shawi, M.K.1    Ketchum, C.J.2    Nakamoto, R.K.3
  • 63
    • 0030680983 scopus 로고    scopus 로고
    • 1-ATP synthase: The uncoupling mutation, γm23K, disrupts the use of binding energy to drive catalysis
    • 1-ATP synthase: the uncoupling mutation, γM23K, disrupts the use of binding energy to drive catalysis Biochemistry 36 1997 12954 12960
    • (1997) Biochemistry , vol.36 , pp. 12954-12960
    • Al-Shawi, M.K.1    Nakamoto, R.K.2
  • 64
    • 0031027579 scopus 로고    scopus 로고
    • 1 ATP synthase are dependent on the energy of interaction between γ and β subunits
    • 1 ATP synthase are dependent on the energy of interaction between γ and β subunits J. Biol. Chem. 272 1997 2300 2306
    • (1997) J. Biol. Chem. , vol.272 , pp. 2300-2306
    • Al-Shawi, M.K.1    Ketchum, C.J.2    Nakamoto, R.K.3
  • 65
    • 0028981359 scopus 로고
    • +-ATPase (ATP synthase): β subunit amino acid replacement suppress a γ subunit mutation having long unrelated carboxyl terminus
    • +-ATPase (ATP synthase): β subunit amino acid replacement suppress a γ subunit mutation having long unrelated carboxyl terminus J. Biol. Chem. 270 1995 22850 22854
    • (1995) J. Biol. Chem. , vol.270 , pp. 22850-22854
    • Jeanteur, C.1    Omote, H.2    Iwamoto-Kihara, A.3    Maeda, M.4    Futai, M.5
  • 67
    • 54449088280 scopus 로고    scopus 로고
    • A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis
    • J.A. Scanlon, M.K. Al-Shawi, and R.K. Nakamoto A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis J. Biol. Chem. 283 2008 26228 26240
    • (2008) J. Biol. Chem. , vol.283 , pp. 26228-26240
    • Scanlon, J.A.1    Al-Shawi, M.K.2    Nakamoto, R.K.3
  • 75
    • 0034708665 scopus 로고    scopus 로고
    • +-ATPase: Preferential expression of the a3 isoform during osteoclast differentiation
    • +-ATPase: preferential expression of the a3 isoform during osteoclast differentiation J. Biol. Chem. 275 2000 8760 8765
    • (2000) J. Biol. Chem. , vol.275 , pp. 8760-8765
    • Toyomura, T.1    Oka, T.2    Yamaguchi, C.3    Wada, Y.4    Futai, M.5
  • 77
    • 84864645945 scopus 로고    scopus 로고
    • Roles and regulatory mechanism of proton pumping V-ATPase in spermatozoa and epididymis physiology
    • Nova Science Publishers
    • M. Nakanishi-Matsui, S. Breton, H. Okamoto, and M. Futai Roles and regulatory mechanism of proton pumping V-ATPase in spermatozoa and epididymis physiology Testis: Anatomy, Physiology and Pathology 2012 Nova Science Publishers
    • (2012) Testis: Anatomy, Physiology and Pathology
    • Nakanishi-Matsui, M.1    Breton, S.2    Okamoto, H.3    Futai, M.4
  • 78
    • 0037413670 scopus 로고    scopus 로고
    • Diversity of mouse proton-translocating ATPase: Presence of multiple isoforms of the C, d and G subunits
    • G.-H. Sun-Wada, T. Yoshimizu, Y. Imai-Senga, Y. Wada, and M. Futai Diversity of mouse proton-translocating ATPase: presence of multiple isoforms of the C, d and G subunits Gene 302 2003 147 153
    • (2003) Gene , vol.302 , pp. 147-153
    • Sun-Wada, G.-H.1    Yoshimizu, T.2    Imai-Senga, Y.3    Wada, Y.4    Futai, M.5
  • 79
    • 0242414411 scopus 로고    scopus 로고
    • Mouse proton pump ATPase C subunit isoforms (C2-a and C2-b) specifically expressed in kidney and lung
    • G.-H. Sun Wada, Y. Murata, M. Namba, A. Yamamoto, Y. Wada, and M. Futai Mouse proton pump ATPase C subunit isoforms (C2-a and C2-b) specifically expressed in kidney and lung J. Biol. Chem. 278 2003 44843 44851
    • (2003) J. Biol. Chem. , vol.278 , pp. 44843-44851
    • Sun Wada, G.-H.1    Murata, Y.2    Namba, M.3    Yamamoto, A.4    Wada, Y.5    Futai, M.6
  • 80
    • 0037124047 scopus 로고    scopus 로고
    • A proton pump ATPase with testis-specific E1 subunit isoform required for acrosome acidification
    • G.-H. Sun-Wada, Y. Imai-Senga, A. Yamamoto, Y. Murata, T. Hirata, Y. Wada, and M. Futai A proton pump ATPase with testis-specific E1 subunit isoform required for acrosome acidification J. Biol. Chem. 277 2002 18098 18105
    • (2002) J. Biol. Chem. , vol.277 , pp. 18098-18105
    • Sun-Wada, G.-H.1    Imai-Senga, Y.2    Yamamoto, A.3    Murata, Y.4    Hirata, T.5    Wada, Y.6    Futai, M.7
  • 86
    • 77955298786 scopus 로고    scopus 로고
    • Domain characterization and interaction of the yeast vacuolar ATPase subunit C with the peripheral stator stalk subunits e and G
    • R.A. Oot, and S. Wilkens Domain characterization and interaction of the yeast vacuolar ATPase subunit C with the peripheral stator stalk subunits E and G J. Biol. Chem. 285 32 2010 24654 24664
    • (2010) J. Biol. Chem. , vol.285 , Issue.32 , pp. 24654-24664
    • Oot, R.A.1    Wilkens, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.