메뉴 건너뛰기




Volumn 8, Issue 1, 2013, Pages

The Torque of Rotary F-ATPase Can Unfold Subunit Gamma If Rotor and Stator Are Cross-Linked

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DISULFIDE; F1 ATPASE SUBUNIT GAMMA; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UNCLASSIFIED DRUG;

EID: 84871880130     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0053754     Document Type: Article
Times cited : (12)

References (33)
  • 1
    • 0028114231 scopus 로고
    • The structure of F1-ATPase from bovine heart mitochondria determined at 2.8 Å resolution
    • Abrahams JP, Leslie AGW, Lutter R, Walker JE, (1994) The structure of F1-ATPase from bovine heart mitochondria determined at 2.8 Å resolution. Nature 370: 621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 2
    • 76049093135 scopus 로고    scopus 로고
    • The structure of the membrane extrinsic region of bovine ATP synthase
    • Rees DM, Leslie AG, Walker JE, (2009) The structure of the membrane extrinsic region of bovine ATP synthase. Proc Natl Acad Sci U S A 106: 21597-21601.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 21597-21601
    • Rees, D.M.1    Leslie, A.G.2    Walker, J.E.3
  • 3
    • 79958858245 scopus 로고    scopus 로고
    • Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation
    • Cingolani G, Duncan TM, (2011) Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation. Nat Struct Mol Biol 18: 701-707.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 701-707
    • Cingolani, G.1    Duncan, T.M.2
  • 4
    • 0034866072 scopus 로고    scopus 로고
    • Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: Torque profile of the enzyme
    • Pänke O, Cherepanov DA, Gumbiowski K, Engelbrecht S, Junge W, (2001) Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: Torque profile of the enzyme. Biophys J 81: 1220-1233.
    • (2001) Biophys J , vol.81 , pp. 1220-1233
    • Pänke, O.1    Cherepanov, D.A.2    Gumbiowski, K.3    Engelbrecht, S.4    Junge, W.5
  • 5
    • 66249132322 scopus 로고    scopus 로고
    • Torque generation and elastic power transmission in the rotary F(O)F(1)-ATPase
    • Junge W, Sielaff H, Engelbrecht S, (2009) Torque generation and elastic power transmission in the rotary F(O)F(1)-ATPase. Nature 459: 364-370.
    • (2009) Nature , vol.459 , pp. 364-370
    • Junge, W.1    Sielaff, H.2    Engelbrecht, S.3
  • 6
    • 48249108462 scopus 로고    scopus 로고
    • Unique rotary ATP synthase and its biological diversity
    • von Ballmoos C, Cook GM, Dimroth P, (2008) Unique rotary ATP synthase and its biological diversity. Annu Rev Biophys 37: 43-64.
    • (2008) Annu Rev Biophys , vol.37 , pp. 43-64
    • von Ballmoos, C.1    Cook, G.M.2    Dimroth, P.3
  • 8
    • 0037188741 scopus 로고    scopus 로고
    • F1-ATPase: The C-terminal end of subunit γ is not required for ATP hydrolysis-driven rotation
    • Müller M, Pänke O, Junge W, Engelbrecht S, (2002) F1-ATPase: The C-terminal end of subunit γ is not required for ATP hydrolysis-driven rotation. J Biol Chem 277: 23308-23313.
    • (2002) J Biol Chem , vol.277 , pp. 23308-23313
    • Müller, M.1    Pänke, O.2    Junge, W.3    Engelbrecht, S.4
  • 9
    • 39349094544 scopus 로고    scopus 로고
    • Axle-less F1-ATPase rotates in the correct direction
    • Furuike S, Hossain MD, Maki Y, Adachi K, Suzuki T, et al. (2008) Axle-less F1-ATPase rotates in the correct direction. Science 319: 955-958.
    • (2008) Science , vol.319 , pp. 955-958
    • Furuike, S.1    Hossain, M.D.2    Maki, Y.3    Adachi, K.4    Suzuki, T.5
  • 10
    • 0033553409 scopus 로고    scopus 로고
    • The 20 C-terminal amino acid residues of the chloroplast ATP synthase γ subunit are not essential for activity
    • Sokolov M, Lu L, Tucker W, Gao F, Gegenheimer PA, et al. (1999) The 20 C-terminal amino acid residues of the chloroplast ATP synthase γ subunit are not essential for activity. J Biol Chem 274: 13824-13829.
    • (1999) J Biol Chem , vol.274 , pp. 13824-13829
    • Sokolov, M.1    Lu, L.2    Tucker, W.3    Gao, F.4    Gegenheimer, P.A.5
  • 11
    • 70350362952 scopus 로고    scopus 로고
    • ATP synthase with its gamma subunit reduced to the N-terminal helix can still catalyze ATP synthesis
    • Mnatsakanyan N, Hook JA, Quisenberry L, Weber J, (2009) ATP synthase with its gamma subunit reduced to the N-terminal helix can still catalyze ATP synthesis. J Biol Chem 284: 26519-26525.
    • (2009) J Biol Chem , vol.284 , pp. 26519-26525
    • Mnatsakanyan, N.1    Hook, J.A.2    Quisenberry, L.3    Weber, J.4
  • 12
    • 58149280492 scopus 로고    scopus 로고
    • Neither helix in the coiled coil region of the axle of F1-ATPase plays a significant role in torque production
    • Hossain MD, Furuike S, Maki Y, Adachi K, Suzuki T, et al. (2008) Neither helix in the coiled coil region of the axle of F1-ATPase plays a significant role in torque production. Biophys J 95: 4837-4844.
    • (2008) Biophys J , vol.95 , pp. 4837-4844
    • Hossain, M.D.1    Furuike, S.2    Maki, Y.3    Adachi, K.4    Suzuki, T.5
  • 13
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F-ATPase
    • Sabbert D, Engelbrecht S, Junge W, (1996) Intersubunit rotation in active F-ATPase. Nature 381: 623-626.
    • (1996) Nature , vol.381 , pp. 623-626
    • Sabbert, D.1    Engelbrecht, S.2    Junge, W.3
  • 14
  • 15
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F-ATPase
    • Noji H, Yasuda R, Yoshida M, Kinosita K, (1997) Direct observation of the rotation of F-ATPase. Nature 386: 299-302.
    • (1997) Nature , vol.386 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita, K.4
  • 17
    • 0035834643 scopus 로고    scopus 로고
    • F-ATPase: forced full rotation of the rotor despite covalent cross-link with the stator
    • Gumbiowski K, Cherepanov D, Müller M, Pänke O, Promto P, et al. (2001) F-ATPase: forced full rotation of the rotor despite covalent cross-link with the stator. J Biol Chem 276: 42287-42292.
    • (2001) J Biol Chem , vol.276 , pp. 42287-42292
    • Gumbiowski, K.1    Cherepanov, D.2    Müller, M.3    Pänke, O.4    Promto, P.5
  • 18
    • 0032540490 scopus 로고    scopus 로고
    • Stability and functionality of cysteine-less F1F0 ATP synthase from Escherichia coli
    • Kuo PH, Ketchum CJ, Nakamoto RK, (1998) Stability and functionality of cysteine-less F1F0 ATP synthase from Escherichia coli. FEBS Lett 426: 217-220.
    • (1998) FEBS Lett , vol.426 , pp. 217-220
    • Kuo, P.H.1    Ketchum, C.J.2    Nakamoto, R.K.3
  • 20
    • 0021736478 scopus 로고
    • In vivo evidence for the role of the epsilon subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli
    • Klionsky DJ, Brusilow WSA, Simoni RD, (1984) In vivo evidence for the role of the epsilon subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli. J Bacteriol 160: 1055-1060.
    • (1984) J Bacteriol , vol.160 , pp. 1055-1060
    • Klionsky, D.J.1    Brusilow, W.S.A.2    Simoni, R.D.3
  • 21
    • 0025340556 scopus 로고
    • Site-directed mutagenesis of the conserved beta subunit tyrosine 331 of Escherichia coli ATP synthase yields catalytically active enzymes
    • Wise JG, (1990) Site-directed mutagenesis of the conserved beta subunit tyrosine 331 of Escherichia coli ATP synthase yields catalytically active enzymes. J Biol Chem 265: 10403-10409.
    • (1990) J Biol Chem , vol.265 , pp. 10403-10409
    • Wise, J.G.1
  • 22
    • 0017390556 scopus 로고
    • A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250
    • Sedmak JJ, Grossberg SE, (1977) A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250. Anal Biochem 79: 544-552.
    • (1977) Anal Biochem , vol.79 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 24
    • 56649088286 scopus 로고    scopus 로고
    • Domain compliance and elastic power transmission in rotary F(O)F(1)-ATPase
    • Sielaff H, Rennekamp H, Wächter A, Xie H, Hilbers F, et al. (2008) Domain compliance and elastic power transmission in rotary F(O)F(1)-ATPase. Proc Natl Acad Sci U S A 105: 17760-17765.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 17760-17765
    • Sielaff, H.1    Rennekamp, H.2    Wächter, A.3    Xie, H.4    Hilbers, F.5
  • 25
    • 79956320744 scopus 로고    scopus 로고
    • Torsional elasticity and energetics of F1-ATPase
    • Czub J, Grubmüller H, (2011) Torsional elasticity and energetics of F1-ATPase. Proc Natl Acad Sci U S A 108: 7408-7413.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 7408-7413
    • Czub, J.1    Grubmüller, H.2
  • 26
    • 79952758006 scopus 로고    scopus 로고
    • Two rotary motors in F-ATP synthase are elastically coupled by a flexible rotor and a stiff stator stalk
    • Wächter A, Bi Y, Dunn SD, Cain BD, Sielaff H, et al. (2011) Two rotary motors in F-ATP synthase are elastically coupled by a flexible rotor and a stiff stator stalk. Proc Natl Acad Sci U S A 108: 3924-3929.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 3924-3929
    • Wächter, A.1    Bi, Y.2    Dunn, S.D.3    Cain, B.D.4    Sielaff, H.5
  • 27
    • 0032947857 scopus 로고    scopus 로고
    • Transient accumulation of elastic energy in proton translocating ATP synthase
    • Cherepanov DA, Mulkidjanian A, Junge W, (1999) Transient accumulation of elastic energy in proton translocating ATP synthase. FEBS Lett 449: 1-6.
    • (1999) FEBS Lett , vol.449 , pp. 1-6
    • Cherepanov, D.A.1    Mulkidjanian, A.2    Junge, W.3
  • 28
    • 17144435428 scopus 로고    scopus 로고
    • Kinetic modeling of rotary CF0F1-ATP synthase: storage of elastic energy during energy transduction
    • Pänke O, Rumberg B, (1999) Kinetic modeling of rotary CF0F1-ATP synthase: storage of elastic energy during energy transduction. Biochim Biophys Acta 1412: 118-128.
    • (1999) Biochim Biophys Acta , vol.1412 , pp. 118-128
    • Pänke, O.1    Rumberg, B.2
  • 29
    • 0035979760 scopus 로고    scopus 로고
    • Inter-subunit rotation and elastic power transmission in FoF1-ATPase
    • Junge W, Pänke O, Cherepanov D, Gumbiowski K, Müller M, et al. (2001) Inter-subunit rotation and elastic power transmission in FoF1-ATPase. FEBS Lett 504: 152-160.
    • (2001) FEBS Lett , vol.504 , pp. 152-160
    • Junge, W.1    Pänke, O.2    Cherepanov, D.3    Gumbiowski, K.4    Müller, M.5
  • 30
    • 0035838982 scopus 로고    scopus 로고
    • Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis
    • Menz RI, Walker JE, Leslie AG, (2001) Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis. Cell 106: 331-341.
    • (2001) Cell , vol.106 , pp. 331-341
    • Menz, R.I.1    Walker, J.E.2    Leslie, A.G.3
  • 31
    • 57149107555 scopus 로고    scopus 로고
    • Cooperative three-step motions in catalytic subunits of F(1)-ATPase correlate with 80 degrees and 40 degrees substep rotations
    • Masaike T, Koyama-Horibe F, Oiwa K, Yoshida M, Nishizaka T, (2008) Cooperative three-step motions in catalytic subunits of F(1)-ATPase correlate with 80 degrees and 40 degrees substep rotations. Nat Struct Mol Biol 15: 1326-1333.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1326-1333
    • Masaike, T.1    Koyama-Horibe, F.2    Oiwa, K.3    Yoshida, M.4    Nishizaka, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.