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Volumn 3, Issue FEB, 2013, Pages

The affinity purification and characterization of ATP synthase complexes from mitochondria

Author keywords

ATP synthase; Coupling; Inhibitor protein; Mitochondria; Purification

Indexed keywords

ADENOSINE TRIPHOSPHATE; ATPASE INHIBITORY PROTEIN; PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; PROTEIN SUBUNIT;

EID: 84877759621     PISSN: None     EISSN: 20462441     Source Type: Journal    
DOI: 10.1098/rsob.120160     Document Type: Article
Times cited : (41)

References (48)
  • 1
    • 0032544312 scopus 로고    scopus 로고
    • ATP synthesis by rotary catalysis
    • doi:10.1002/(SICI)1521-3773(19980918) 37:17,2308::AIDANIE2308.3.0.CO;2-W
    • Walker JE. 1998 ATP synthesis by rotary catalysis. Angew. Chem. Int. Ed. 37, 5000-5011. (doi:10.1002/(SICI)1521-3773(19980918)37:17,2308::AIDANIE2308.3. 0.CO;2-W)
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 5000-5011
    • Walker, J.E.1
  • 2
    • 84873120174 scopus 로고    scopus 로고
    • The ATP synthase: The understood, the uncertain and the unknown
    • doi:10.1042/BST20110773
    • Walker JE. 2012 The ATP synthase: the understood, the uncertain and the unknown. Biochem. Soc. Trans. 41, 1-16. (doi:10.1042/BST20110773)
    • (2012) Biochem. Soc. Trans. , vol.41 , pp. 1-16
    • Walker, J.E.1
  • 3
  • 7
    • 0035838982 scopus 로고    scopus 로고
    • 1-ATPase with nucleotide bound to all three catalytic sites: Implications for the mechanism of rotary catalysis
    • DOI 10.1016/S0092-8674(01)00452-4
    • 1-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis. Cell 106, 331-341. (doi:10.1016/S0092-8674(01)00452-4) (Pubitemid 32772617)
    • (2001) Cell , vol.106 , Issue.3 , pp. 331-341
    • Menz R.Ian1    Walker, J.E.2    Leslie, A.G.W.3
  • 8
    • 33745548556 scopus 로고    scopus 로고
    • On the structure of the stator of the mitochondrial ATP synthase
    • DOI 10.1038/sj.emboj.7601177, PII 7601177
    • Dickson VK, Silvester JA, Fearnley IM, Leslie AGW, Walker JE. 2006 On the structure of the stator of the mitochondrial ATP synthase. EMBO J. 25, 2911-2918. (doi:10.1038/sj.emboj.7601177) (Pubitemid 43980397)
    • (2006) EMBO Journal , vol.25 , Issue.12 , pp. 2911-2918
    • Dickson, V.K.1    Silvester, J.A.2    Fearnley, I.M.3    Leslie, A.G.W.4    Walker, J.E.5
  • 9
    • 76049093135 scopus 로고    scopus 로고
    • The structure of the membrane extrinsic region of bovine ATP synthase
    • doi:10.1073/pnas.0910365106
    • Rees DM, Leslie AGW, Walker JE. 2009 The structure of the membrane extrinsic region of bovine ATP synthase. Proc. Natl Acad. Sci. USA 106, 21 597-21 601. (doi:10.1073/pnas.0910365106)
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 21597-21601
    • Rees, D.M.1    Leslie, A.G.W.2    Walker, J.E.3
  • 10
    • 78049288139 scopus 로고    scopus 로고
    • Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria
    • doi:10.1073/pnas.1011099107
    • Watt IN, Montgomery MG, Runswick MJ, Leslie AGW, Walker JE. 2010 Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria. Proc. Natl Acad. Sci. USA 107, 16 823-16 827. (doi:10.1073/pnas. 1011099107)
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 16823-16827
    • Watt, I.N.1    Montgomery, M.G.2    Runswick, M.J.3    Leslie, A.G.W.4    Walker, J.E.5
  • 11
    • 0347504884 scopus 로고    scopus 로고
    • Structure of the mitochondrial ATP synthase by electron cryomicroscopy
    • DOI 10.1093/emboj/cdg608
    • Rubinstein JL, Walker JE, Henderson R. 2003 Structure of the mitochondrial ATP synthase by electron cryomicroscopy. EMBO J. 22, 6182-6192. (doi:10.1093/emboj/cdg608) (Pubitemid 37522576)
    • (2003) EMBO Journal , vol.22 , Issue.23 , pp. 6182-6192
    • Rubinstein, J.L.1    Walker, J.E.2    Henderson, R.3
  • 12
    • 84863959033 scopus 로고    scopus 로고
    • 1-ATPase from bovine heart mitochondria
    • doi:10.1073/pnas.1207587109
    • Rees DM, Montgomery MG, Leslie AGW, Walker JE. 2012 Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria. Proc. Natl Acad. Sci. USA 109, 11 139-11 143. (doi:10.1073/pnas.1207587109)
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 11139-11143
    • Rees, D.M.1    Montgomery, M.G.2    Leslie, A.G.W.3    Walker, J.E.4
  • 16
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D, Leslie AGW, Walker JE. 1999 Molecular architecture of the rotary motor in ATP synthase. Science 286, 1700-1705. (doi:10.1126/science.286.5445. 1700) (Pubitemid 129515869)
    • (1999) Science , vol.286 , Issue.5445 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 17
    • 0000228422 scopus 로고
    • A soluble heat stable protein in mitochondria from bovine heart that inhibits ATP hydrolase activity
    • Pullman ME, Monroy GC. 1963 A soluble heat stable protein in mitochondria from bovine heart that inhibits ATP hydrolase activity. J. Biol. Chem. 238, 3762-3769.
    • (1963) J. Biol. Chem. , vol.238 , pp. 3762-3769
    • Pullman, M.E.1    Monroy, G.C.2
  • 19
    • 0037126590 scopus 로고    scopus 로고
    • 1, the regulatory subunit of mitochondrial F-ATPase
    • DOI 10.1093/emboj/20.24.6990
    • 1, the regulatory subunit of mitochondrial F-ATPase. EMBO J. 20, 6990-6996. (doi:10.1093/emboj/20.24.6990) (Pubitemid 34062291)
    • (2001) EMBO Journal , vol.20 , Issue.24 , pp. 6990-6996
    • Cabezon, E.1    Runswick, M.J.2    Leslie, A.G.W.3    Walker, J.E.4
  • 22
    • 0001728083 scopus 로고
    • Partial resolution of the enzymes catalysing oxidative phosphorylation: Purification and properties of soluble, dinitrophenol-stimulated adenosine triphosphatase
    • Pullman ME, Penefsky H, Datta A, Racker E. 1960 Partial resolution of the enzymes catalysing oxidative phosphorylation: purification and properties of soluble, dinitrophenol-stimulated adenosine triphosphatase. J. Biol. Chem. 235, 3322-3329.
    • (1960) J. Biol. Chem. , vol.235 , pp. 3322-3329
    • Pullman, M.E.1    Penefsky, H.2    Datta, A.3    Racker, E.4
  • 23
    • 77957003097 scopus 로고
    • Preparation, properties and conditions for assay of mitochondria: Slaughterhouse material, small-scale
    • doi:10.1016/0076-6879(67)10016-5
    • Smith AL. 1967 Preparation, properties and conditions for assay of mitochondria: slaughterhouse material, small-scale. Methods Enzymol. 10, 81-86. (doi:10.1016/0076-6879(67)10016-5)
    • (1967) Methods Enzymol. , vol.10 , pp. 81-86
    • Smith, A.L.1
  • 24
    • 0014216716 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation. 13. Structure and function of submitochondrial particles completely resolved with respect to coupling factor
    • Racker E, Horstman LL. 1967 Partial resolution of the enzymes catalyzing oxidative phosphorylation. 13. Structure and function of submitochondrial particles completely resolved with respect to coupling factor. J. Biol. Chem. 242, 2547-2551.
    • (1967) J. Biol. Chem. , vol.242 , pp. 2547-2551
    • Racker, E.1    Horstman, L.L.2
  • 28
    • 70349787152 scopus 로고    scopus 로고
    • Measurement of the molecular masses of hydrophilic and hydrophobic subunits of ATP synthase and complex i in a single experiment
    • doi:10.1016/j.ab.2009.08.006
    • Carroll J, Fearnley IM, Wang Q, Walker JE. 2009 Measurement of the molecular masses of hydrophilic and hydrophobic subunits of ATP synthase and complex I in a single experiment. Anal. Biochem. 395, 249-255. (doi:10.1016/j.ab.2009.08.006)
    • (2009) Anal. Biochem. , vol.395 , pp. 249-255
    • Carroll, J.1    Fearnley, I.M.2    Wang, Q.3    Walker, J.E.4
  • 29
    • 0029897240 scopus 로고    scopus 로고
    • Unidirectional reconstitution into detergent-destabilized liposomes of the purified lactose transport system of Streptococcus thermophilus
    • DOI 10.1074/jbc.271.26.15358
    • Knol J, Veenhoff L, Liang WJ, Henderson PJ, Leblanc G, Poolman B. 1996 Unidirectional reconstitution into detergent-destabilized liposomes of the purified lactose transport system of Streptococcus thermophilus. J. Biol. Chem. 271, 15 358-15 366. (doi:10.1074/jbc.271.26.15358) (Pubitemid 26225303)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.26 , pp. 15358-15366
    • Knol, J.1    Veenhoff, L.2    Liang, W.-J.3    Henderson, P.J.F.4    Leblanc, G.5    Poolman, B.6
  • 30
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • doi:10.1016/0076-6879(74)31072-5
    • Oesterhelt D, Stoeckenius W. 1974 Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 31, 667-678. (doi:10.1016/0076-6879(74)31072-5)
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 31
    • 0014717442 scopus 로고
    • Possible regulatory function of a mitochondrial ATPase inhibitor in respiratory chain-linked energy transfer
    • doi:10.1016/0005-2728(70)90261-6
    • Asami K, Juniti K, Ernster L. 1970 Possible regulatory function of a mitochondrial ATPase inhibitor in respiratory chain-linked energy transfer. Biochim. Biophys. Acta 205, 307-311. (doi:10.1016/0005-2728(70)90261-6)
    • (1970) Biochim. Biophys. Acta , vol.205 , pp. 307-311
    • Asami, K.1    Juniti, K.2    Ernster, L.3
  • 32
    • 0016432003 scopus 로고
    • Stimulation of rat liver mitochondrial adenosine triphosphatase by anions
    • Ebel RE, Lardy HA. 1975 Stimulation of rat liver mitochondrial adenosine triphosphatase by anions. J. Biol. Chem. 250, 191-196.
    • (1975) J. Biol. Chem. , vol.250 , pp. 191-196
    • Ebel, R.E.1    Lardy, H.A.2
  • 33
    • 0020069242 scopus 로고
    • Kinetic mechanism of mitochondrial adenosine triphosphatase. Inhibition by azide and activation by sulphite
    • Vasilyeva EA, Minkov IB, Fitin AF, Vinogradov AD. 1982 Kinetic mechanism of mitochondrial adenosine triphosphatase: inhibition by azide and activation by sulphite. Biochem. J. 202, 15-23. (Pubitemid 12139169)
    • (1982) Biochemical Journal , vol.202 , Issue.1 , pp. 15-23
    • Vasilyeva, E.A.1    Minkov, I.B.2    Fitin, A.F.3    Vinogradov, A.D.4
  • 34
    • 34250886311 scopus 로고    scopus 로고
    • Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria
    • DOI 10.1016/j.febslet.2007.05.079, PII S001457930700631X
    • Chen R, Runswick MJ, Carroll J, Fearnley IM, Walker JE. 2007 Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria. FEBS Lett. 581, 3145-3148. (doi:10.1016/j.febslet.2007.05.079) (Pubitemid 46977353)
    • (2007) FEBS Letters , vol.581 , Issue.17 , pp. 3145-3148
    • Chen, R.1    Runswick, M.J.2    Carroll, J.3    Fearnley, I.M.4    Walker, J.E.5
  • 35
    • 0029808314 scopus 로고    scopus 로고
    • ATP synthase of yeast mitochondria. Isolation of the subunit h and disruption of the ATP14 gene
    • DOI 10.1074/jbc.271.34.20284
    • Arselin G, Vaillier J, Graves PV, Velours J. 1996 ATP synthase of yeast mitochondria: isolation of the subunit h and disruption of the ATP14 gene. J. Biol. Chem. 271, 20 284-20 290. (doi:10.1074/jbc.271.34.20284) (Pubitemid 26281793)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.34 , pp. 20284-20290
    • Arselin, G.1    Vaillier, J.2    Graves, P.-V.3    Velours, J.4
  • 36
    • 0022490783 scopus 로고
    • Amino acid substitutions in mitochondrial ATPase subunit 9 of Saccharomyces cerevisiae leading to oligomycin or venturicidin resistance
    • DOI 10.1016/0014-5793(86)80152-1
    • Nagley P, Hall RM, Ooi BG. 1986 Amino acid substitutions in mitochondrial ATPase subunit 9 of Saccharomyces cerevisiae leading to oligomycin or venturicidin resistance. FEBS Lett. 195, 159-163. (doi:10.1016/0014-5793(86) 80152-1) (Pubitemid 16048994)
    • (1986) FEBS Letters , vol.195 , Issue.1-2 , pp. 159-163
    • Nagley, P.1    Hall, R.M.2    Ooi, B.G.3
  • 37
    • 84865544585 scopus 로고    scopus 로고
    • Oligomycin frames a common drug-binding site in the ATP synthase
    • doi:10.1073/pnas.1207912109
    • Symersky J, Osowski D, Walters DE, Mueller DM. 2012 Oligomycin frames a common drug-binding site in the ATP synthase. Proc. Natl Acad. Sci. USA 109, 13 961-13 965. (doi:10.1073/pnas.1207912109)
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 13961-13965
    • Symersky, J.1    Osowski, D.2    Walters, D.E.3    Mueller, D.M.4
  • 38
    • 0015209679 scopus 로고
    • Enzymic characterization and lipid composition of rat liver subcellular membranes
    • doi:10.1016/0005-2736(71)90123-4
    • Colbeau A, Nachbaur J, Vignais PM. 1971 Enzymic characterization and lipid composition of rat liver subcellular membranes. Biochim. Biophys. Acta 249, 462-492. (doi:10.1016/0005-2736(71)90123-4)
    • (1971) Biochim. Biophys. Acta , vol.249 , pp. 462-492
    • Colbeau, A.1    Nachbaur, J.2    Vignais, P.M.3
  • 39
    • 0029009125 scopus 로고
    • Isolation and biochemical characterization of organelles from the yeast, Saccharomyces cerevisiae
    • doi:10.1002/yea.320110602
    • Zinser E, Daum G. 1995 Isolation and biochemical characterization of organelles from the yeast, Saccharomyces cerevisiae. Yeast 11, 493-536. (doi:10.1002/yea.320110602)
    • (1995) Yeast , vol.11 , pp. 493-536
    • Zinser, E.1    Daum, G.2
  • 40
    • 0028588948 scopus 로고
    • The regulation of catalysis in ATP synthase
    • doi:10.1016/0959-440X(94)90274-7
    • Walker JE. 1994 The regulation of catalysis in ATP synthase. Curr. Opin. Struct. Biol. 4, 912-918. (doi:10.1016/0959-440X(94)90274-7)
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 912-918
    • Walker, J.E.1
  • 41
    • 0029817347 scopus 로고    scopus 로고
    • 0-ATPase and complex I from bovine heart mitochondria
    • o-ATPase and complex I from bovine heart mitochondria. Biochem. J. 318, 343-349. (Pubitemid 26283665)
    • (1996) Biochemical Journal , vol.318 , Issue.1 , pp. 343-349
    • Buchanan, S.K.1    Walker, J.E.2
  • 42
    • 0015969754 scopus 로고
    • Reconstitution of purple membrane vesicles catalyzing light-driven proton uptake and adenosine triphosphate formation
    • Racker E, Stoeckenius W. 1974 Reconstitution of purple membrane vesicles catalyzing light-driven proton uptake and adenosine triphosphate formation. J. Biol. Chem. 249, 662-663.
    • (1974) J. Biol. Chem. , vol.249 , pp. 662-663
    • Racker, E.1    Stoeckenius, W.2
  • 43
    • 0014027487 scopus 로고
    • Partial resolution of the enzymes catalysing oxidative phosphorylation. X. Correlation of morphology and function in submitochondrial particles
    • Kagawa Y, Racker E. 1966 Partial resolution of the enzymes catalysing oxidative phosphorylation. X. Correlation of morphology and function in submitochondrial particles. J. Biol. Chem. 241, 2475-2482.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2475-2482
    • Kagawa, Y.1    Racker, E.2
  • 44
    • 0014027518 scopus 로고
    • Partial resolution of the enzymes catalysing oxidative phosphorylation. IX. Reconstitution of oligomycin-sensitive adenosine triphosphatase
    • Kagawa Y, Racker E. 1966 Partial resolution of the enzymes catalysing oxidative phosphorylation. IX. Reconstitution of oligomycin-sensitive adenosine triphosphatase. J. Biol. Chem. 241, 2467-2474.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2467-2474
    • Kagawa, Y.1    Racker, E.2
  • 46
    • 0028301141 scopus 로고
    • 0-ATPases
    • DOI 10.1016/0014-5793(94)00368-8
    • o-ATPases. FEBS Lett. 346, 39-43. (doi:10.1016/0014-5793(94)00368-8) (Pubitemid 24183824)
    • (1994) FEBS Letters , vol.346 , Issue.1 , pp. 39-43
    • Walker, J.E.1
  • 47
    • 33745713048 scopus 로고    scopus 로고
    • The peripheral stalk of the mitochondrial ATP synthase
    • DOI 10.1016/j.bbabio.2006.01.001, PII S0005272806000028
    • Walker JE, Dickson VK. 2006 The peripheral stalk of the mitochondrial ATP synthase. Biochim. Biophys. Acta 1757, 286-296. (doi:10.1016/j.bbabio.2006.01. 001) (Pubitemid 43996944)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.5-6 , pp. 286-296
    • Walker, J.E.1    Dickson, V.K.2
  • 48
    • 84863955498 scopus 로고    scopus 로고
    • Arrangement of subunits in intact mammalian mitochondrial ATP synthase determined by cryo-EM
    • doi:10.1073/pnas.1204935109
    • Baker LA, Watt IN, Runswick MJ, Walker JE, Rubinstein JL. 2012 Arrangement of subunits in intact mammalian mitochondrial ATP synthase determined by cryo-EM. Proc. Natl Acad. Sci. USA 109, 11 675-11 680. (doi:10.1073/pnas.1204935109)
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 11675-11680
    • Baker, L.A.1    Watt, I.N.2    Runswick, M.J.3    Walker, J.E.4    Rubinstein, J.L.5


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