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Volumn 442, Issue 3, 2012, Pages 631-638

Functional analysis of membranous F o-a subunit of F 1F o-ATP synthase by in vitro protein synthesis

Author keywords

A subunit; Cell free protein synthesis; F 1F o ATP synthase (F 1F o); H + pump; Membrane protein; Proteoliposome

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALANINE; ARGININE; ASPARAGINE; ASPARTIC ACID; GLUTAMINE; LIPOSOME; MEMBRANE PROTEIN; PROTEINASE; PROTON; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 84863242790     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20111284     Document Type: Article
Times cited : (44)

References (49)
  • 1
    • 0037131230 scopus 로고    scopus 로고
    • A research journey with ATP synthase
    • Boyer, P. D. (2002) A research journey with ATP synthase. J. Biol. Chem. 277, 39045-39061
    • (2002) J. Biol. Chem. , vol.277 , pp. 39045-39061
    • Boyer, P.D.1
  • 2
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotatory mechanics
    • DOI 10.1016/S0968-0004(97)01129-8, PII S0968000497011298
    • Junge, W., Lill, H. and Engelbrecht, S. (1997) ATP synthase: an electrochemical transducer with rotatory mechanics. Trends Biochem. Sci. 22, 420-423 (Pubitemid 27508785)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.11 , pp. 420-423
    • Junge, W.1    Lill, H.2    Engelbrecht, S.3
  • 4
    • 0032568845 scopus 로고    scopus 로고
    • 0ATP synthase as determined by labeling of unique cysteine residues
    • 0ATP synthase as determined by labeling of unique cysteine residues. J. Biol. Chem. 273, 16235-16240
    • (1998) J. Biol. Chem. , vol.273 , pp. 16235-16240
    • Long, J.C.1    Wang, S.2    Vik, S.B.3
  • 5
    • 0032568818 scopus 로고    scopus 로고
    • 0 ATP synthase
    • DOI 10.1074/jbc.273.26.16241
    • Valiyaveetil, F. I. and Fillingame, R. H. (1998) Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase. J. Biol. Chem. 273, 16241-16247 (Pubitemid 28311400)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.26 , pp. 16241-16247
    • Valiyaveetil, F.I.1    Fillingame, R.H.2
  • 6
    • 0033546193 scopus 로고    scopus 로고
    • A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase
    • Wada, T., Long, J. C., Zhang, D. and Vik, S. B. (1999) A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase. J. Biol. Chem. 274, 17353-17357
    • (1999) J. Biol. Chem. , vol.274 , pp. 17353-17357
    • Wada, T.1    Long, J.C.2    Zhang, D.3    Vik, S.B.4
  • 9
    • 0028086470 scopus 로고
    • 0-ATP synthase
    • Wang, S. and Vik, S. B. (1994) Single amino acid insertions probe the α subunit of the Escherichia coli F1F0-ATP synthase. J. Biol. Chem. 269, 3095-3099 (Pubitemid 24235821)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.4 , pp. 3095-3099
    • Wang, S.1    Vik, S.B.2
  • 10
    • 0024977998 scopus 로고
    • 0ATPase of Escherichia coli. Mutagenic analysis of the a subunit
    • 0ATPase of Escherichia coli. Mutagenic analysis of the a subunit. J. Biol. Chem. 264, 3292-3300
    • (1989) J. Biol. Chem. , vol.264 , pp. 3292-3300
    • Cain, B.D.1    Simoni, R.D.2
  • 14
    • 42449112499 scopus 로고    scopus 로고
    • Arginine-induced conformational change in the c-ring/a-subunit interface of ATP synthase
    • DOI 10.1111/j.1742-4658.2008.06368.x
    • Vorburger, T., Ebneter, J. Z., Wiedenmann, A., Morger, D., Weber, G., Diederichs, K., Dimroth, P. and von Ballmoos, C. (2008) Arginine-induced conformational change in the c-ring/a-subunit interface of ATP synthase. FEBS J. 275, 2137-2150 (Pubitemid 351569554)
    • (2008) FEBS Journal , vol.275 , Issue.9 , pp. 2137-2150
    • Vorburger, T.1    Ebneter, J.Z.2    Wiedenmann, A.3    Morger, D.4    Weber, G.5    Diederichs, K.6    Dimroth, P.7    Von Ballmoos, C.8
  • 16
    • 0037809269 scopus 로고    scopus 로고
    • Close proximity of a cytoplasmic loop of subunit a with c subunits of the ATP synthase from Escherichia coli
    • DOI 10.1074/jbc.M212413200
    • Zhang, D. and Vik, S. B. (2003) Close proximity of a cytoplasmic loop of subunit a with c subunits of the ATP synthase from Escherichia coli. J. Biol. Chem. 278, 12319-12324 (Pubitemid 36800215)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 12319-12324
    • Zhang, D.1    Vik, S.B.2
  • 17
    • 0037458716 scopus 로고    scopus 로고
    • Aqueous access channels in subunit a of rotary ATP synthase
    • DOI 10.1074/jbc.M210199200
    • Angevine, C. M. and Fillingame, R. H. (2003) Aqueous access channels in subunit a of rotary ATP synthase. J. Biol. Chem. 278, 6066-6074 (Pubitemid 36800858)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.8 , pp. 6066-6074
    • Angevine, C.M.1    Fillingame, R.H.2
  • 18
    • 34247877574 scopus 로고    scopus 로고
    • Aqueous access pathways in ATP synthase subunit a: Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5
    • DOI 10.1074/jbc.M610848200
    • Angevine, C. M., Herold, K. A., Vincent, O. D. and Fillingame, R. H. (2007) Aqueous access pathways in ATP synthase subunit a . Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5. J. Biol. Chem. 282, 9001-9007 (Pubitemid 47093514)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.12 , pp. 9001-9007
    • Angevine, C.M.1    Herold, K.A.G.2    Vincent, O.D.3    Fillingame, R.H.4
  • 19
    • 45149117135 scopus 로고    scopus 로고
    • The cytoplasmic loops of subunit a of Escherichia coli ATP synthase may participate in the proton translocating mechanism
    • Moore, K. J., Angevine, C. M., Vincent, O. D., Schwem, B. E. and Fillingame, R. H. (2008) The cytoplasmic loops of subunit a of Escherichia coli ATP synthase may participate in the proton translocating mechanism. J. Biol. Chem. 283, 13044-13052
    • (2008) J. Biol. Chem. , vol.283 , pp. 13044-13052
    • Moore, K.J.1    Angevine, C.M.2    Vincent, O.D.3    Schwem, B.E.4    Fillingame, R.H.5
  • 21
    • 0029047850 scopus 로고
    • Identification of functionally important helical faces in transmembrane segments by scanning mutagenesis
    • Lee, G. F., Dutton, D. P. and Hazelbauer, G. L. (1995) Identification of functionally important helical faces in transmembrane segments by scanning mutagenesis. Proc. Natl. Acad. Sci. U.S.A. 92, 5416-5420
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5416-5420
    • Lee, G.F.1    Dutton, D.P.2    Hazelbauer, G.L.3
  • 22
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C. L., Omura, S. and Kopito, R. R. (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83, 121-127
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 23
    • 0029989855 scopus 로고    scopus 로고
    • FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins
    • DOI 10.1074/jbc.271.49.31196
    • Akiyama, Y., Kihara, A., Tokuda, H. and Ito, K. (1996) FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins. J. Biol. Chem. 271, 31196-31201 (Pubitemid 26408563)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.49 , pp. 31196-31201
    • Akiyama, Y.1    Kihara, A.2    Tokuda, H.3    Ito, K.4
  • 24
    • 0033485546 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis provides no evidence for the extracellular accessibility of the nucleotide-binding domains of the multidrug resistance transporter P-glycoprotein
    • Blott, E. J., Higgins, C. F. and Linton, K. J. (1999) Cysteine-scanning mutagenesis provides no evidence for the extracellular accessibility of the nucleotide-binding domains of the multidrug resistance transporter P-glycoprotein. EMBO J. 18, 6800-6808
    • (1999) EMBO J. , vol.18 , pp. 6800-6808
    • Blott, E.J.1    Higgins, C.F.2    Linton, K.J.3
  • 25
    • 4544273344 scopus 로고    scopus 로고
    • +-pyrophosphatase of Streptomyces coelicolor determined by cysteine-scanning mutagenesis
    • +-pyrophosphatase of Streptomyces coelicolor determined by cysteine-scanning mutagenesis. J. Biol. Chem. 279, 35106-35112
    • (2004) J. Biol. Chem. , vol.279 , pp. 35106-35112
    • Mimura, H.1    Nakanishi, Y.2    Hirono, M.3    Maeshima, M.4
  • 26
    • 2642549055 scopus 로고    scopus 로고
    • Structure and function of extracellular loop 4 of the serotonin transporter as revealed by cysteine-scanning mutagenesis
    • DOI 10.1074/jbc.M311173200
    • Mitchell, S. M., Lee, E., Garcia, M. L. and Stephan, M. M. (2004) Structure and function of extracellular loop 4 of the serotonin transporter as revealed by cysteine-scanning mutagenesis. J. Biol. Chem. 279, 24089-24099 (Pubitemid 38725268)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.23 , pp. 24089-24099
    • Mitchell, S.M.1    Lee, E.2    Garcia, M.L.3    Stephan, M.M.4
  • 27
    • 34447630299 scopus 로고    scopus 로고
    • Functional Cell-free Synthesis of a Seven Helix Membrane Protein: In situ Insertion of Bacteriorhodopsin into Liposomes
    • DOI 10.1016/j.jmb.2007.05.087, PII S0022283607007589
    • Kalmbach, R., Chizhov, I., Schumacher, M. C., Friedrich, T., Bamberg, E. and Engelhard, M. (2007) Functional cell-free synthesis of a seven helix membrane protein: in situ insertion of bacteriorhodopsin into liposomes. J. Mol. Biol. 371, 639-648 (Pubitemid 47087829)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.3 , pp. 639-648
    • Kalmbach, R.1    Chizhov, I.2    Schumacher, M.C.3    Friedrich, T.4    Bamberg, E.5    Engelhard, M.6
  • 30
    • 54049126868 scopus 로고    scopus 로고
    • Wheat germ cell-free translation, purification, and assembly of a functional human stearoyl-CoA desaturase complex
    • Goren, M. A. and Fox, B. G. (2008) Wheat germ cell-free translation, purification, and assembly of a functional human stearoyl-CoA desaturase complex. Protein Expr. Purif. 62, 171-178
    • (2008) Protein Expr. Purif. , vol.62 , pp. 171-178
    • Goren, M.A.1    Fox, B.G.2
  • 33
    • 69249095799 scopus 로고    scopus 로고
    • Cell-free synthesis of functional aquaporin Z in synthetic liposomes
    • Hovijitra, N. T., Wuu, J. J., Peaker, B. and Swartz, J. R. (2009) Cell-free synthesis of functional aquaporin Z in synthetic liposomes. Biotechnol. Bioeng. 104, 40-49
    • (2009) Biotechnol. Bioeng. , vol.104 , pp. 40-49
    • Hovijitra, N.T.1    Wuu, J.J.2    Peaker, B.3    Swartz, J.R.4
  • 34
    • 77958544345 scopus 로고    scopus 로고
    • Preparative scale production of functional mouse aquaporin 4 using different cell-free expression modes
    • Kai, L., Kaldenhoff, R., Lian, J., Zhu, X., Dötsch, V., Bernhard, F., Cen, P. and Xu, Z. (2010) Preparative scale production of functional mouse aquaporin 4 using different cell-free expression modes. PLoS ONE 5, e12972
    • (2010) PLoS ONE , vol.5
    • Kai, L.1    Kaldenhoff, R.2    Lian, J.3    Zhu, X.4    Dötsch, V.5    Bernhard, F.6    Cen, P.7    Xu, Z.8
  • 35
    • 79551687349 scopus 로고    scopus 로고
    • M13 procoat protein insertion into YidC and SecYEG proteoliposomes and liposomes
    • Stiegler, N., Dalbey, R. E. and Kuhn, A. (2011) M13 procoat protein insertion into YidC and SecYEG proteoliposomes and liposomes. J. Mol. Biol. 406, 362-370
    • (2011) J. Mol. Biol. , vol.406 , pp. 362-370
    • Stiegler, N.1    Dalbey, R.E.2    Kuhn, A.3
  • 37
    • 78649788244 scopus 로고    scopus 로고
    • Efficient cell-free expression with the endogenous E. coli RNA polymerase and sigma factor 70
    • Shin, J. and Noireaux, V. (2010) Efficient cell-free expression with the endogenous E. coli RNA polymerase and sigma factor 70. J. Biol. Eng. 4, 8
    • (2010) J. Biol. Eng. , vol.4 , pp. 8
    • Shin, J.1    Noireaux, V.2
  • 38
    • 59249084001 scopus 로고    scopus 로고
    • A synthetic biology approach to the construction of membrane proteins in semi-synthetic minimal cells
    • Kuruma, Y., Stano, P., Ueda, T. and Luisi, P. L. (2009) A synthetic biology approach to the construction of membrane proteins in semi-synthetic minimal cells. Biochim. Biophys. Acta 1788, 567-574
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 567-574
    • Kuruma, Y.1    Stano, P.2    Ueda, T.3    Luisi, P.L.4
  • 39
    • 63149130741 scopus 로고    scopus 로고
    • Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins
    • Niwa, T., Ying, B. W., Saito, K., Jin, W., Takada, S., Ueda, T. and Taguchi, H. (2009) Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins. Proc. Natl. Acad. Sci. U.S.A. 106, 4201-4206
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 4201-4206
    • Niwa, T.1    Ying, B.W.2    Saito, K.3    Jin, W.4    Takada, S.5    Ueda, T.6    Taguchi, H.7
  • 40
    • 66749151526 scopus 로고    scopus 로고
    • Epitope mapping using ribosome display in a reconstituted cell-free protein synthesis system
    • Osada, E., Shimizu, Y., Akbar, B. K., Kanamori, T. and Ueda, T. (2009) Epitope mapping using ribosome display in a reconstituted cell-free protein synthesis system. J. Biochem. 145, 693-700
    • (2009) J. Biochem. , vol.145 , pp. 693-700
    • Osada, E.1    Shimizu, Y.2    Akbar, B.K.3    Kanamori, T.4    Ueda, T.5
  • 42
    • 0037066772 scopus 로고    scopus 로고
    • oof ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring
    • o of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring. J. Biol. Chem. 277, 13281-13285
    • (2002) J. Biol. Chem. , vol.277 , pp. 13281-13285
    • Suzuki, T.1    Ueno, H.2    Mitome, N.3    Suzuki, J.4    Yoshida, M.5
  • 44
    • 76249120489 scopus 로고    scopus 로고
    • Conformational transitions of subunit epsilon in ATP synthase from thermophilic Bacillus PS3
    • Feniouk, B. A., Kato-Yamada, Y., Yoshida, M. and Suzuki, T. (2010) Conformational transitions of subunit epsilon in ATP synthase from thermophilic Bacillus PS3. Biophys. J. 98, 434-442
    • (2010) Biophys. J. , vol.98 , pp. 434-442
    • Feniouk, B.A.1    Kato-Yamada, Y.2    Yoshida, M.3    Suzuki, T.4
  • 45
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock, D., Leslie, A. G. and Walker, J. E. (1999) Molecular architecture of the rotary motor in ATP synthase. Science 286, 1700-1705 (Pubitemid 129515869)
    • (1999) Science , vol.286 , Issue.5445 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 47
  • 48
    • 79960591989 scopus 로고    scopus 로고
    • Efficient ATP synthesis by thermophilic Bacillus FoF1-ATP synthase
    • Soga, N., Kinoshita, Jr, K., Yoshida, M. and Suzuki, T. (2011) Efficient ATP synthesis by thermophilic Bacillus FoF1-ATP synthase. FEBS J. 278, 2647-2654
    • (2011) FEBS J. , vol.278 , pp. 2647-2654
    • Soga, N.1    Kinoshita Jr., K.2    Yoshida, M.3    Suzuki, T.4


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