메뉴 건너뛰기




Volumn 1618, Issue 1, 2003, Pages 59-66

Characterisation of subunit III and its oligomer from spinach chloroplast ATP synthase

Author keywords

CD spectroscopy; FTIR; MALDI mass spectrometry; Membrane protein

Indexed keywords

DODECYL SULFATE SODIUM; OLIGOMER; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; VEGETABLE PROTEIN;

EID: 0345708278     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2003.10.007     Document Type: Article
Times cited : (16)

References (41)
  • 2
    • 84943704466 scopus 로고
    • Isolation and characterization of a supramolecular complex of subunit III of the ATP synthase from chloroplasts
    • Fromme P., Boekema E.J., Gräber P. Isolation and characterization of a supramolecular complex of subunit III of the ATP synthase from chloroplasts. Z. Naturforsch., C. 42c:1987;1239-1245.
    • (1987) Z. Naturforsch., C , vol.42 , pp. 1239-1245
    • Fromme, P.1    Boekema, E.J.2    Gräber, P.3
  • 4
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F-ATPase
    • Sabbert D., Engelbrecht S., Junge W. Intersubunit rotation in active F-ATPase. Nature. 381:1996;623-625.
    • (1996) Nature , vol.381 , pp. 623-625
    • Sabbert, D.1    Engelbrecht, S.2    Junge, W.3
  • 7
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D., Leslie A.G., Walker J.E. 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.2    Walker, J.E.3
  • 10
    • 0035838982 scopus 로고    scopus 로고
    • 1-ATPase with nucleotide bound to all three catalytic sites: Implications for the mechanism of rotary catalysis
    • 1-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis. Cell. 106:2001;331-341.
    • (2001) Cell , vol.106 , pp. 331-341
    • Menz, R.I.1    Walker, J.E.2    Leslie, A.G.3
  • 12
    • 0035846822 scopus 로고    scopus 로고
    • 1-ATPase at 3.2Å resolution
    • 1-ATPase at 3.2Å resolution. J. Biol. Chem. 276:2001;1345-1352.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1345-1352
    • Groth, G.1    Pohl, E.2
  • 13
    • 0037133559 scopus 로고    scopus 로고
    • 1-ATPase complexed with the phytopathogenic inhibitor tentoxin
    • 1-ATPase complexed with the phytopathogenic inhibitor tentoxin. Proc. Natl. Acad. Sci. U. S. A. 99:2002;3464-3468.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 3464-3468
    • Groth, G.1
  • 18
    • 0141757507 scopus 로고    scopus 로고
    • Fourteen protomers compose the oligomer III of the proton-rotor in spinach chloroplast ATP synthase
    • Seelert H., Dencher N.A., Müller D.J. Fourteen protomers compose the oligomer III of the proton-rotor in spinach chloroplast ATP synthase. J. Mol. Biol. 333:2003;337-344.
    • (2003) J. Mol. Biol. , vol.333 , pp. 337-344
    • Seelert, H.1    Dencher, N.A.2    Müller, D.J.3
  • 19
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • Rastogi V.K., Girvin M.E. Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature. 402:1999;263-268.
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi, V.K.1    Girvin, M.E.2
  • 21
    • 0018800747 scopus 로고
    • Purification and reconstitution of the N,N′- dicyclohexylcarbodiimide-sensitive ATPase complex from spinach chloroplasts
    • Pick U., Racker E. Purification and reconstitution of the N,N′-dicyclohexylcarbodiimide-sensitive ATPase complex from spinach chloroplasts. J. Biol. Chem. 254:1979;2793-2799.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2793-2799
    • Pick, U.1    Racker, E.2
  • 22
    • 0018063082 scopus 로고
    • Characterization of the dicyclohexylcarbodiimide-binding protein isolated from chloroplast membranes
    • Sigrist-Nelson K., Sigrist H., Azzi A. Characterization of the dicyclohexylcarbodiimide-binding protein isolated from chloroplast membranes. Eur. J. Biochem. 92:1978;9-14.
    • (1978) Eur. J. Biochem. , vol.92 , pp. 9-14
    • Sigrist-Nelson, K.1    Sigrist, H.2    Azzi, A.3
  • 23
    • 85030944451 scopus 로고
    • Bochum: Ruhr-Universität Bochum
    • Klein-Hitpass L. Biologie. 1983;Ruhr-Universität Bochum, Bochum.
    • (1983) Biologie
    • Klein-Hitpass, L.1
  • 25
    • 0018436335 scopus 로고
    • Purification of the chloroplast-membrane dicyclohexylcarbodi-imide- binding proteolipid by ion-exchange chromatography
    • Sigrist-Nelson K., Azzi A. Purification of the chloroplast-membrane dicyclohexylcarbodi-imide-binding proteolipid by ion-exchange chromatography. Biochem. J. 177:1979;687-692.
    • (1979) Biochem. J. , vol.177 , pp. 687-692
    • Sigrist-Nelson, K.1    Azzi, A.2
  • 26
    • 0000544299 scopus 로고
    • A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels
    • Oakley B.R., Kirsch D.R., Morris N.R. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal. Biochem. 105:1980;361-363.
    • (1980) Anal. Biochem. , vol.105 , pp. 361-363
    • Oakley, B.R.1    Kirsch, D.R.2    Morris, N.R.3
  • 27
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68:1996;850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 28
    • 0019487684 scopus 로고
    • Glycoprotein molecular-weight estimation using sodium dodecyl sulfate-pore gradient electrophoresis: Comparison of tris-glycine and tris-borate-EDTA buffer systems
    • Poduslo J.F. Glycoprotein molecular-weight estimation using sodium dodecyl sulfate-pore gradient electrophoresis: comparison of tris-glycine and tris-borate-EDTA buffer systems. Anal. Biochem. 114:1981;131-139.
    • (1981) Anal. Biochem. , vol.114 , pp. 131-139
    • Poduslo, J.F.1
  • 29
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Andersen J. Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J. Biochem. Biophys. Methods. 10:1984;203-209.
    • (1984) J. Biochem. Biophys. Methods , vol.10 , pp. 203-209
    • Kyhse-Andersen, J.1
  • 30
    • 0029963631 scopus 로고    scopus 로고
    • Calcium binding to the subunit c of E. coli ATP-synthase and possible functional implications in energy coupling
    • Zakharov S.D., Li X., Red'ko T.P., Dilley R.A. Calcium binding to the subunit c of E. coli ATP-synthase and possible functional implications in energy coupling. J. Bioenerg. Biomembranes. 28:1996;483-494.
    • (1996) J. Bioenerg. Biomembranes , vol.28 , pp. 483-494
    • Zakharov, S.D.1    Li, X.2    Red'Ko, T.P.3    Dilley, R.A.4
  • 31
    • 0018118041 scopus 로고
    • Circular dichroic analysis of protein conformation: Inclusion of the beta-turns
    • Chang C.T., Wu C.S., Yang J.T. Circular dichroic analysis of protein conformation: inclusion of the beta-turns. Anal. Biochem. 91:1978;13-31.
    • (1978) Anal. Biochem. , vol.91 , pp. 13-31
    • Chang, C.T.1    Wu, C.S.2    Yang, J.T.3
  • 32
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton L.A., Johnson W.C. Jr. Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 155:1986;155-167.
    • (1986) Anal. Biochem. , vol.155 , pp. 155-167
    • Compton, L.A.1    Johnson, W.C.Jr.2
  • 33
    • 0032961627 scopus 로고    scopus 로고
    • Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: A method for the removal of silver ions to enhance sensitivity
    • Gharahdaghi F., Weinberg C.R., Meagher D.A., Imai B.S., Mische S.M. Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: a method for the removal of silver ions to enhance sensitivity. Electrophoresis. 20:1999;601-605.
    • (1999) Electrophoresis , vol.20 , pp. 601-605
    • Gharahdaghi, F.1    Weinberg, C.R.2    Meagher, D.A.3    Imai, B.S.4    Mische, S.M.5
  • 36
    • 0037181463 scopus 로고    scopus 로고
    • Self-assembly of ATP synthase subunit c rings
    • Arechaga I., Butler P.J., Walker J.E. Self-assembly of ATP synthase subunit c rings. FEBS Lett. 515:2002;189-193.
    • (2002) FEBS Lett. , vol.515 , pp. 189-193
    • Arechaga, I.1    Butler, P.J.2    Walker, J.E.3
  • 38
    • 0030851913 scopus 로고    scopus 로고
    • O-ATPase of Propionigenium modestum-production, purification and properties of the protein in dodecylsulfate solution
    • O-ATPase of Propionigenium modestum-production, purification and properties of the protein in dodecylsulfate solution. Eur. J. Biochem. 247:1997;820-825.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 820-825
    • Matthey, U.1    Kaim, G.2    Dimroth, P.3
  • 39
    • 0020492959 scopus 로고
    • Folding of the mitochondrial proton adenosinetriphosphatase proteolipid channel in phospholipid vesicles
    • Mao D., Wachter E., Wallace B.A. Folding of the mitochondrial proton adenosinetriphosphatase proteolipid channel in phospholipid vesicles. Biochemistry. 21:1982;4960-4968.
    • (1982) Biochemistry , vol.21 , pp. 4960-4968
    • Mao, D.1    Wachter, E.2    Wallace, B.A.3
  • 40
    • 0028971414 scopus 로고
    • Matrix-assisted laser desorption/ionization mass-spectrometry (MALDI-MS) of membrane-proteins and noncovalent complexes
    • Rosinke B., Strupat K., Hillenkamp F., Rosenbusch J., Dencher N., Krüger U., Galla H.J. Matrix-assisted laser desorption/ionization mass-spectrometry (MALDI-MS) of membrane-proteins and noncovalent complexes. J. Mass Spectrom. 30:1995;1462-1468.
    • (1995) J. Mass Spectrom. , vol.30 , pp. 1462-1468
    • Rosinke, B.1    Strupat, K.2    Hillenkamp, F.3    Rosenbusch, J.4    Dencher, N.5    Krüger, U.6    Galla, H.J.7
  • 41
    • 0037056021 scopus 로고    scopus 로고
    • Combined in-gel tryptic digestion and CNBr cleavage for the generation of peptide maps of an integral membrane protein with MALDI-TOF mass spectrometry
    • van Montfort B.A., Doeven M.K., Canas B., Veenhoff L.M., Poolman B., Robillard G.T. Combined in-gel tryptic digestion and CNBr cleavage for the generation of peptide maps of an integral membrane protein with MALDI-TOF mass spectrometry. Biochim. Biophys. Acta. 1555:2002;111-115.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 111-115
    • Van Montfort, B.A.1    Doeven, M.K.2    Canas, B.3    Veenhoff, L.M.4    Poolman, B.5    Robillard, G.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.