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Volumn 108, Issue 37, 2011, Pages 15196-15200

Interaction of complexes I, III, and IV within the bovine respirasome by single particle cryoelectron tomography

Author keywords

Electron microscopy; Oxidative phosphorylation

Indexed keywords

CYTOCHROME C; CYTOCHROME C OXIDASE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); RESPIRASOME; UBIQUINOL CYTOCHROME C REDUCTASE; UNCLASSIFIED DRUG;

EID: 80053073046     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1107819108     Document Type: Article
Times cited : (153)

References (37)
  • 1
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schägger H, Pfeiffer K (2000) Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J 19:1777-1783. (Pubitemid 30204389)
    • (2000) EMBO Journal , vol.19 , Issue.8 , pp. 1777-1783
    • Schagger, H.1    Pfeiffer, K.2
  • 4
    • 26844548023 scopus 로고    scopus 로고
    • Structure of dimeric ATP synthase from mitochondria: An angular association of monomers induces the strong curvature of the inner membrane
    • DOI 10.1016/j.febslet.2005.09.065, PII S001457930501183X
    • Dudkina NV, Heinemeyer J, Keegstra W, Boekema EJ, Braun HP (2005) Structure of dimeric ATP synthase frommitochondria: An angular association of monomers induces the strong curvature of the inner membrane. FEBS Lett 579:5769-5772. (Pubitemid 41455662)
    • (2005) FEBS Letters , vol.579 , Issue.25 , pp. 5769-5772
    • Dudkina, N.V.1    Heinemeyer, J.2    Keegstra, W.3    Boekema, E.J.4    Braun, H.-P.5
  • 6
    • 77951912692 scopus 로고    scopus 로고
    • 3.3 Å Cryo-EM structure of a non-enveloped virus reveals a priming mechanism for cell entry
    • Zhang X, Jin L, Fang Q, Wong HH, Zhou ZH (2010) 3.3 Å Cryo-EM structure of a non-enveloped virus reveals a priming mechanism for cell entry. Cell 141:472-482.
    • (2010) Cell , vol.141 , pp. 472-482
    • Zhang, X.1    Jin, L.2    Fang, Q.3    Wong, H.H.4    Zhou, Z.H.5
  • 7
    • 0023102907 scopus 로고
    • Angular reconstitution-a posteriori assignment of projection directions for 3-D reconstitution
    • Van Heel M (1987) Angular reconstitution-a posteriori assignment of projection directions for 3-D reconstitution. Ultramicroscopy 21:111-123.
    • (1987) Ultramicroscopy , vol.21 , pp. 111-123
    • Van Heel, M.1
  • 8
    • 84985231782 scopus 로고
    • Three-dimensional reconstruction from a single-exposure, random-conical tilt series applied to the 50S ribosomal subunit of Escherichia coli
    • Radermacher M, Wagenknecht T, Verschoor A, Frank J (1987) Three-dimensional reconstruction from a single-exposure, random-conical tilt series applied to the 50S ribosomal subunit of Escherichia coli. J Microsc 146:113-136.
    • (1987) J Microsc , vol.146 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 10
    • 34948891095 scopus 로고    scopus 로고
    • Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
    • DOI 10.1038/nature06170, PII NATURE06170
    • Beck M, Lucic V, Forster F, Baumeister W, Medalia O (2007) Snapshots of nuclear pore complexes in action captured by cryoelectron tomography. Nature 449:611-615. (Pubitemid 47525150)
    • (2007) Nature , vol.449 , Issue.7162 , pp. 611-615
    • Beck, M.1    Lui, V.2    Forster, F.3    Baumeister, W.4    Medalia, O.5
  • 11
    • 71049139404 scopus 로고    scopus 로고
    • Averaging of electron subtomograms and random conical tilt reconstructions through likelihood optimization
    • Scheres SH, Melero R, Valle M, Carazo JM (2009) Averaging of electron subtomograms and random conical tilt reconstructions through likelihood optimization. Structure 17:1563-1572.
    • (2009) Structure , vol.17 , pp. 1563-1572
    • Scheres, S.H.1    Melero, R.2    Valle, M.3    Carazo, J.M.4
  • 13
    • 0029942862 scopus 로고    scopus 로고
    • The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å
    • Tsukihara T, et al. (1996) The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272:1136-1144.
    • (1996) Science , vol.272 , pp. 1136-1144
    • Tsukihara, T.1
  • 14
    • 77954848120 scopus 로고    scopus 로고
    • Functional modules and structural basis of conformational coupling in mitochondrial complex I
    • Hunte C, Zickermann V, Brandt U (2010) Functional modules and structural basis of conformational coupling in mitochondrial complex I. Science 329:448-451.
    • (2010) Science , vol.329 , pp. 448-451
    • Hunte, C.1    Zickermann, V.2    Brandt, U.3
  • 15
    • 33847232164 scopus 로고    scopus 로고
    • Structure determination in situ by averaging of tomograms
    • Förster F, Hegerl R (2007) Structure determination in situ by averaging of tomograms. Methods Cell Biol 79:741-767.
    • (2007) Methods Cell Biol , vol.79 , pp. 741-767
    • Förster, F.1    Hegerl, R.2
  • 16
    • 35848929504 scopus 로고    scopus 로고
    • 1 from bovine heart mitochondria
    • DOI 10.1021/bi700983h
    • Schäfer E, Dencher NA, Vonck J, Parcej DN (2007) Three-dimensional structure of the respiratory chain supercomplex I1III2IV1 from bovine heartmitochondria. Biochemistry 46:12579-12585. (Pubitemid 350060084)
    • (2007) Biochemistry , vol.46 , Issue.44 , pp. 12579-12585
    • Schafer, E.1    Dencher, N.A.2    Vonck, J.3    Parcej, D.N.4
  • 17
    • 78649908437 scopus 로고    scopus 로고
    • Maximum likelihood based classification of electron tomographic data
    • Stölken M, et al. (2011) Maximum likelihood based classification of electron tomographic data. J Struct Biol 173:77-85.
    • (2011) J Struct Biol , vol.173 , pp. 77-85
    • Stölken, M.1
  • 18
  • 19
    • 79651473928 scopus 로고    scopus 로고
    • Fine structure of granal thylakoid membrane organization using cryoelectron tomography
    • Kouřil R, Oostergetel GT, Boekema EJ (2011) Fine structure of granal thylakoid membrane organization using cryoelectron tomography. Biochim Biophys Acta 1807:368-374.
    • (2011) Biochim Biophys Acta , vol.1807 , pp. 368-374
    • Kouřil, R.1    Oostergetel, G.T.2    Boekema, E.J.3
  • 21
    • 34548425430 scopus 로고    scopus 로고
    • A maximum likelihood approach to two-dimensional crystals
    • DOI 10.1016/j.jsb.2007.09.013, PII S1047847707002304, Electron Crystallography of Membrane Proteins
    • Zeng X, Stahlberg H, Grigorieff N (2007) A maximum likelihood approach to two-dimensional crystals. J Struct Biol 160:362-374. (Pubitemid 350101248)
    • (2007) Journal of Structural Biology , vol.160 , Issue.3 , pp. 362-374
    • Zeng, X.1    Stahlberg, H.2    Grigorieff, N.3
  • 22
    • 0033780164 scopus 로고    scopus 로고
    • Fitting atomic models into electron-microscopy maps
    • Rossmann MG (2000) Fitting atomic models into electron-microscopy maps. Acta Crystallogr D Biol Crystallogr 56:1341-1349.
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , pp. 1341-1349
    • Rossmann, M.G.1
  • 23
    • 34249688217 scopus 로고    scopus 로고
    • A structural model of the cytochrome c reductase/oxidase supercomplex from yeast mitochondria
    • DOI 10.1074/jbc.M610545200
    • Heinemeyer J, Braun HP, Boekema EJ, Kouřil R (2007) A structural model of the cytochrome C reductase/oxidase supercomplex from yeast mitochondria. J Biol Chem 282:12240-12248. (Pubitemid 47100694)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.16 , pp. 12240-12248
    • Heinemeyer, J.1    Braun, H.-P.2    Boekema, E.J.3    Kouril, R.4
  • 24
    • 0037113864 scopus 로고    scopus 로고
    • Gluing the respiratory chain together: Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane
    • DOI 10.1074/jbc.C200551200
    • Zhang M, Mileykovskaya E, Dowhan W (2002) Gluing the respiratory chain together Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane. J Biol Chem 277:43553-43556. (Pubitemid 36157767)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.46 , pp. 43553-43556
    • Zhang, M.1    Mileykovskaya, E.2    Dowhan, W.3
  • 25
    • 66749192576 scopus 로고    scopus 로고
    • 1 complex catalysis and supercomplex formation
    • 1 complex catalysis and supercomplex formation. Biochim Biophys Acta 1787:609-616.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 609-616
    • Wenz, T.1
  • 26
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial photosystem II at 2.9-Å resolution and the role of quinones, lipids, channels and chloride
    • Guskov A, et al. (2009) Cyanobacterial photosystem II at 2.9-Å resolution and the role of quinones, lipids, channels and chloride. Nat Struct Mol Biol 16:334-342.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 334-342
    • Guskov, A.1
  • 27
    • 77952979824 scopus 로고    scopus 로고
    • The architecture of respiratory complex I
    • Efremov RG, Baradaran R, Sazanov LA (2010) The architecture of respiratory complex I. Nature 465:441-445.
    • (2010) Nature , vol.465 , pp. 441-445
    • Efremov, R.G.1    Baradaran, R.2    Sazanov, L.A.3
  • 28
    • 0021815336 scopus 로고
    • Mobility in the mitochondrial electron transport chain
    • DOI 10.1021/bi00331a017
    • Hochman J, Ferguson-Miller S, Schindler M (1985) Mobility in the mitochondrial electron transfer chain. Biochemistry 24:2509-2516. (Pubitemid 15015757)
    • (1985) Biochemistry , vol.24 , Issue.10 , pp. 2509-2516
    • Hochman, J.1    Ferguson-Miller, S.2    Schindler, M.3
  • 29
    • 4344561983 scopus 로고    scopus 로고
    • The mitochondrial respiratory chain is partially organized in a supercomplex assembly: Kinetic evidence using flux control analysis
    • DOI 10.1074/jbc.M405135200
    • Bianchi C, Genova ML, Parenti Castelli G, Lenaz G (2004) The mitochondrial respiratory chain is partially organized in a supercomplex assembly: Kinetic evidence using flux control analysis. J Biol Chem 279:36562-36569. (Pubitemid 39128999)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.35 , pp. 36562-36569
    • Blanchi, C.1    Genova, M.L.2    Castelli, G.P.3    Lenaz, G.4
  • 31
    • 33748986546 scopus 로고    scopus 로고
    • Supercomplexes and subcomplexes of mitochondrial oxidative phosphorylation
    • DOI 10.1016/j.bbabio.2006.05.006, PII S0005272806001307, Mitochondria: from Molecular Insight to Physiology and Pathology
    • Wittig I, Carrozzo R, Santorelli FM, Schägger H (2006) Supercomplexes and subcomplexes of mitochondrial oxidative phosphorylation. Biochim Biophys Acta 1757:1066-1072. (Pubitemid 44442118)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.9-10 , pp. 1066-1072
    • Wittig, I.1    Carrozzo, R.2    Santorelli, F.M.3    Schagger, H.4
  • 32
    • 57649211340 scopus 로고    scopus 로고
    • Megacomplex organization of the oxidative phosphorylation system by structural analysis of respiratory supercomplexes from potato
    • Bultema JB, Braun HP, Boekema EJ, Kouřil R (2009) Megacomplex organization of the oxidative phosphorylation system by structural analysis of respiratory supercomplexes from potato. Biochim Biophys Acta 1787:60-67.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 60-67
    • Bultema, J.B.1    Braun, H.P.2    Boekema, E.J.3    Kouřil, R.4
  • 33
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel T, Holbrook NJ (2000) Oxidants, oxidative stress and the biology of ageing. Nature 408:239-247.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 34
    • 0036119404 scopus 로고    scopus 로고
    • Biochemical dissection of the mitochondrial proteome from Arabidopsis thaliana by three-dimensional gel electrophoresis
    • DOI 10.1002/1522-2683(200202)23:4<640::AID-ELPS640>3.0.CO;2-F
    • Werhahn W, Braun HP (2002) Biochemical dissection of the mitochondrial proteome from Arabidopsis thaliana by three-dimensional gel electrophoresis. Electrophoresis 23:640-646. (Pubitemid 34232966)
    • (2002) Electrophoresis , vol.23 , Issue.4 , pp. 640-646
    • Werhahn, W.1    Braun, H.-P.2
  • 35
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • DOI 10.1006/jsbi.1996.0013
    • Kremer JR, Mastronarde DN, McIntosh JR (1996) Computer visualization of three dimensional image data using IMOD. J Struct Biol 116:71-76. (Pubitemid 26093126)
    • (1996) Journal of Structural Biology , vol.116 , Issue.1 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 36
    • 25144494651 scopus 로고    scopus 로고
    • Fourier shell correlation threshold criteria
    • DOI 10.1016/j.jsb.2005.05.009, PII S1047847705001292
    • Van Heel M, Schatz M (2005) Fourier shell correlation threshold criteria. J Struct Biol 151:250-262. (Pubitemid 41338732)
    • (2005) Journal of Structural Biology , vol.151 , Issue.3 , pp. 250-262
    • Van Heel, M.1    Schatz, M.2
  • 37
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera - a visualization system for exploratory research and analysis. J Comput Chem 25:1605-1612.
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


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