메뉴 건너뛰기




Volumn 1607, Issue 2-3, 2003, Pages 167-179

FRET reveals changes in the F1-stator stalk interaction during activity of F1F0-ATP synthase

Author keywords

ATP synthase; Fluorescent protein; FRET; GFP; Stator stalk

Indexed keywords

ADENOSINE PHOSPHATE; ASPARAGINE; FUNGAL PROTEIN; GLYCINE; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; OLIGOMYCIN SENSITIVITY CONFERRING PROTEIN; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UNCLASSIFIED DRUG;

EID: 0344196915     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.09.013     Document Type: Article
Times cited : (26)

References (48)
  • 1
    • 0034738103 scopus 로고    scopus 로고
    • Insights into ATP synthase assembly and function through the molecular genetic manipulation of subunits of the yeast mitochondrial enzyme complex
    • Devenish R.J., Prescott M., Roucou X., Nagley P. Insights into ATP synthase assembly and function through the molecular genetic manipulation of subunits of the yeast mitochondrial enzyme complex. Biochim. Biophys. Acta. 1458:2000;428-442.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 428-442
    • Devenish, R.J.1    Prescott, M.2    Roucou, X.3    Nagley, P.4
  • 2
    • 0036496185 scopus 로고    scopus 로고
    • Mechanism of the F(1)F(0)-type ATP synthase, a biological rotary motor
    • Capaldi R.A., Aggeler R. Mechanism of the F(1)F(0)-type ATP synthase, a biological rotary motor. Trends Biochem. Sci. 27:2002;154-160.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 154-160
    • Capaldi, R.A.1    Aggeler, R.2
  • 3
    • 0029807877 scopus 로고    scopus 로고
    • 3 oligomer fixed by OSCP-b stator via the β DELSEED sequence
    • 3 oligomer fixed by OSCP-b stator via the β DELSEED sequence. J. Bioenerg. Biomembranes. 28:1996;421-431.
    • (1996) J. Bioenerg. Biomembranes , vol.28 , pp. 421-431
    • Kagawa, Y.1    Hamamoto, T.2
  • 4
    • 2642707545 scopus 로고    scopus 로고
    • ATP synthase's second stalk comes into focus
    • Wilkens S., Capaldi R.A. ATP synthase's second stalk comes into focus. Nature. 393:1998;29.
    • (1998) Nature , vol.393 , pp. 29
    • Wilkens, S.1    Capaldi, R.A.2
  • 6
    • 0033538506 scopus 로고    scopus 로고
    • Novel features in the structure of bovine ATP synthase
    • Karrasch S., Walker J.E. Novel features in the structure of bovine ATP synthase. J. Mol. Biol. 290:1999;379-384.
    • (1999) J. Mol. Biol. , vol.290 , pp. 379-384
    • Karrasch, S.1    Walker, J.E.2
  • 7
    • 0032947857 scopus 로고    scopus 로고
    • Transient accumulation of elastic energy in proton translocating ATP synthase
    • Cherepanov D.A., Mulkidjanian A.Y., Junge W. Transient accumulation of elastic energy in proton translocating ATP synthase. FEBS Lett. 449:1999;1-6.
    • (1999) FEBS Lett. , vol.449 , pp. 1-6
    • Cherepanov, D.A.1    Mulkidjanian, A.Y.2    Junge, W.3
  • 9
    • 0033971704 scopus 로고    scopus 로고
    • Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase
    • Capaldi R.A., Schulenberg B., Murray J., Aggeler R. Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase. J. Exp. Biol. 203:2000;29-33.
    • (2000) J. Exp. Biol. , vol.203 , pp. 29-33
    • Capaldi, R.A.1    Schulenberg, B.2    Murray, J.3    Aggeler, R.4
  • 10
    • 0035812687 scopus 로고    scopus 로고
    • ATP synthase motor components: Proposal and animation of two dynamic models for stator function
    • Blum D.J., Ko Y.H., Hong S., Rini D.A., Pedersen P.L. ATP synthase motor components: proposal and animation of two dynamic models for stator function. Biochem. Biophys. Res. Commun. 287:2001;801-807.
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 801-807
    • Blum, D.J.1    Ko, Y.H.2    Hong, S.3    Rini, D.A.4    Pedersen, P.L.5
  • 11
    • 0032575052 scopus 로고    scopus 로고
    • The assembly of yeast mitochondrial ATP synthase: Subunit depletion in vivo suggests ordered assembly of the stalk subunits b, OSCP and d
    • Straffon A.F., Prescott M., Nagley P., Devenish R.J. The assembly of yeast mitochondrial ATP synthase: subunit depletion in vivo suggests ordered assembly of the stalk subunits b, OSCP and d. Biochim. Biophys. Acta. 137:1998;157-162.
    • (1998) Biochim. Biophys. Acta , vol.137 , pp. 157-162
    • Straffon, A.F.1    Prescott, M.2    Nagley, P.3    Devenish, R.J.4
  • 12
    • 0033548491 scopus 로고    scopus 로고
    • Single copies of subunits d, oligomycin-sensitivity conferring protein, and b are present in the Saccharomyces cerevisiae mitochondrial ATP synthase
    • Bateson M., Devenish R.J., Nagley P., Prescott M. Single copies of subunits d, oligomycin-sensitivity conferring protein, and b are present in the Saccharomyces cerevisiae mitochondrial ATP synthase. J. Biol. Chem. 274:1999;7462-7466.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7462-7466
    • Bateson, M.1    Devenish, R.J.2    Nagley, P.3    Prescott, M.4
  • 13
    • 0033755689 scopus 로고    scopus 로고
    • Topology and proximity relationships of yeast mitochondrial ATP synthase subunit 8 determined by unique introduced cysteine residues
    • Stephens A.N., Roucou X., Artika I.M., Devenish R.J., Nagley P. Topology and proximity relationships of yeast mitochondrial ATP synthase subunit 8 determined by unique introduced cysteine residues. Eur. J. Biochem. 267:2000;6443-6451.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6443-6451
    • Stephens, A.N.1    Roucou, X.2    Artika, I.M.3    Devenish, R.J.4    Nagley, P.5
  • 18
    • 0034695406 scopus 로고    scopus 로고
    • Localization of the δ subunit in the Escherichia coli F(1)F(0)-ATP synthase by immuno electron microscopy: The δ subunit binds on top of the F(1)
    • Wilkens S., Zhou J., Nakayama R., Dunn S.D., Capaldi R.A. Localization of the δ subunit in the Escherichia coli F(1)F(0)-ATP synthase by immuno electron microscopy: the δ subunit binds on top of the F(1). J. Mol. Biol. 295:2000;387-391.
    • (2000) J. Mol. Biol. , vol.295 , pp. 387-391
    • Wilkens, S.1    Zhou, J.2    Nakayama, R.3    Dunn, S.D.4    Capaldi, R.A.5
  • 19
    • 0030462222 scopus 로고    scopus 로고
    • Cross-linking of engineered subunit δ to (αβ)3 in chloroplast F-ATPase
    • Lill H., Hensel F., Junge W., Engelbrecht S. Cross-linking of engineered subunit δ to (αβ)3 in chloroplast F-ATPase. J. Biol. Chem. 271:1996;32737-32742.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32737-32742
    • Lill, H.1    Hensel, F.2    Junge, W.3    Engelbrecht, S.4
  • 22
    • 0034221877 scopus 로고    scopus 로고
    • 0 connections in the bovine mitochondrial ATP synthase: The role of the α subunit N-terminus, oligomycin- sensitivity conferring protein (OSCP) and subunit d
    • 0 connections in the bovine mitochondrial ATP synthase: the role of the α subunit N-terminus, oligomycin-sensitivity conferring protein (OSCP) and subunit d. Eur. J. Biochem. 267:2000;4445-4455.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4445-4455
    • Xu, T.1    Zanotti, F.2    Gaballo, A.3    Raho, G.4    Papa, S.5
  • 23
    • 0036971192 scopus 로고    scopus 로고
    • ATP Synthase from Saccharomyces cerevisiae: Location of the OSCP subunit in the peripheral stalk region
    • Rubinstein J.L., Walker J.E. ATP Synthase from Saccharomyces cerevisiae: location of the OSCP subunit in the peripheral stalk region. J. Mol. Biol. 321:2002;613-619.
    • (2002) J. Mol. Biol. , vol.321 , pp. 613-619
    • Rubinstein, J.L.1    Walker, J.E.2
  • 24
    • 0027048722 scopus 로고
    • Heterologous expression, purification, and biochemistry of the oligomycin sensitivity conferring protein (OSCP) from yeast
    • Mukhopadhyay A., Zhou X.Q., Uh M., Mueller D.M. Heterologous expression, purification, and biochemistry of the oligomycin sensitivity conferring protein (OSCP) from yeast. J. Biol. Chem. 267:1992;5690-5696.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5690-5696
    • Mukhopadhyay, A.1    Zhou, X.Q.2    Uh, M.3    Mueller, D.M.4
  • 27
    • 0034468767 scopus 로고    scopus 로고
    • 0-ATP synthase by variants of the oligomycin sensitivity-conferring protein containing substitutions near the C-terminus
    • 0-ATP synthase by variants of the oligomycin sensitivity-conferring protein containing substitutions near the C-terminus. J. Bioenerg. Biomembranes. 32:2000;469-481.
    • (2000) J. Bioenerg. Biomembranes , vol.32 , pp. 469-481
    • Boyle, G.M.1    Roucou, X.2    Nagley, P.3    Devenish, R.J.4    Prescott, M.5
  • 28
    • 0030610646 scopus 로고    scopus 로고
    • Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin
    • Miyawaki A., Llopis J., Heim R., McCaffery J., Adams J., Ikura M., Tsien R. Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin. Nature. 388:1997;882-887.
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1    Llopis, J.2    Heim, R.3    McCaffery, J.4    Adams, J.5    Ikura, M.6    Tsien, R.7
  • 29
    • 0031865351 scopus 로고    scopus 로고
    • Bcl-2 and Bax interactions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer
    • Mahajan N., Linder K., Berry G., Gordon G., Heim R., Herman B. Bcl-2 and Bax interactions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer. Nat. Biotechnol. 16:1998;522-547.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 522-547
    • Mahajan, N.1    Linder, K.2    Berry, G.3    Gordon, G.4    Heim, R.5    Herman, B.6
  • 30
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski R.S., Hieter P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:1989;19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 31
    • 0033543597 scopus 로고    scopus 로고
    • The length of polypeptide linker affects the stability of green fluorescent protein fusion proteins
    • Prescott M., Nowakowski S., Nagley P., Devenish R.J. The length of polypeptide linker affects the stability of green fluorescent protein fusion proteins. Anal. Biochem. 273:1999;305-307.
    • (1999) Anal. Biochem. , vol.273 , pp. 305-307
    • Prescott, M.1    Nowakowski, S.2    Nagley, P.3    Devenish, R.J.4
  • 33
    • 0025979877 scopus 로고
    • Targeting, disruption, replacement, and allele rescue: Integrative DNA transformation in yeast
    • Rothstein R. Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol. 194:1991;281-301.
    • (1991) Methods Enzymol. , vol.194 , pp. 281-301
    • Rothstein, R.1
  • 34
    • 0021668558 scopus 로고
    • A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance
    • Boeke J.D., LaCroute F., Fink G.R. A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance. Mol. Gen. Genet. 197:1984;345-346.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 345-346
    • Boeke, J.D.1    Lacroute, F.2    Fink, G.R.3
  • 35
    • 0026090063 scopus 로고
    • In vitro mutagenesis and plasmid shuffling: From cloned gene to mutant yeast
    • Sikorski R.S., Boeke J.D. In vitro mutagenesis and plasmid shuffling: from cloned gene to mutant yeast. Methods Enzymol. 194:1991;302-318.
    • (1991) Methods Enzymol. , vol.194 , pp. 302-318
    • Sikorski, R.S.1    Boeke, J.D.2
  • 37
    • 0018793062 scopus 로고
    • -s mutations in the oli2 region of mitochondrial DNA affecting the 20 000 dalton subunit of the mitochondrial ATPase in Saccharomyces cerevisiae
    • -s mutations in the oli2 region of mitochondrial DNA affecting the 20. 000 dalton subunit of the mitochondrial ATPase in Saccharomyces cerevisiae FEBS Lett. 108:1979;501-504.
    • (1979) FEBS Lett. , vol.108 , pp. 501-504
    • Roberts, H.1    Choo, W.M.2    Murphy, M.3    Marzuki, S.4    Lukins, H.B.5    Linnane, A.W.6
  • 38
    • 0032867611 scopus 로고    scopus 로고
    • Phosphorylation of ribosomal protein L18 is required for its folding and binding to 5S rRNA
    • Bloemink M.J., Moore P.B. Phosphorylation of ribosomal protein L18 is required for its folding and binding to 5S rRNA. Biochemistry. 38:1999;13385-13390.
    • (1999) Biochemistry , vol.38 , pp. 13385-13390
    • Bloemink, M.J.1    Moore, P.B.2
  • 40
    • 0025039056 scopus 로고
    • The gene coding for the yeast oligomycin sensitivity-conferring protein
    • Uh M., Jones D., Mueller D.M. The gene coding for the yeast oligomycin sensitivity-conferring protein. J. Biol. Chem. 265:1990;19047-19052.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19047-19052
    • Uh, M.1    Jones, D.2    Mueller, D.M.3
  • 41
    • 0029995389 scopus 로고    scopus 로고
    • Entrapment by immobilized metal ion affinity chromatography of assembled yeast mitochondrial ATP synthase containing individual subunits tagged with hexahistidine
    • Bateson M., Devenish R.J., Nagley P., Prescott M. Entrapment by immobilized metal ion affinity chromatography of assembled yeast mitochondrial ATP synthase containing individual subunits tagged with hexahistidine. Anal. Biochem. 238:1996;14-18.
    • (1996) Anal. Biochem. , vol.238 , pp. 14-18
    • Bateson, M.1    Devenish, R.J.2    Nagley, P.3    Prescott, M.4
  • 42
    • 0001881653 scopus 로고    scopus 로고
    • Biochemical and physical properties of green fluorescent protein
    • M. Chalfie, & S. Kain. New York: Wiley-Liss
    • Ward W.W. Biochemical and physical properties of green fluorescent protein. Chalfie M., Kain S. Green Fluorescent Protein: Properties, Applications and Protocols. 1998;45-75 Wiley-Liss, New York.
    • (1998) Green Fluorescent Protein: Properties, Applications and Protocols , pp. 45-75
    • Ward, W.W.1
  • 43
    • 0019820370 scopus 로고
    • Purification and immunological properties of proton-ATPase complexes from yeast and rat liver mitochondria
    • Rott R., Nelson N. Purification and immunological properties of proton-ATPase complexes from yeast and rat liver mitochondria. J. Biol. Chem. 256:1981;9224-9228.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9224-9228
    • Rott, R.1    Nelson, N.2
  • 44
    • 0034681280 scopus 로고    scopus 로고
    • Direct visualisation of conformational changes in EF(0)F(1) by electron microscopy
    • Bottcher B., Bertsche I., Reuter R., Graber P. Direct visualisation of conformational changes in EF(0)F(1) by electron microscopy. J. Mol. Biol. 296:2000;449-457.
    • (2000) J. Mol. Biol. , vol.296 , pp. 449-457
    • Bottcher, B.1    Bertsche, I.2    Reuter, R.3    Graber, P.4
  • 47
    • 0036434301 scopus 로고    scopus 로고
    • An approach for reducing unwanted oligomerisation of DsRed fusion proteins
    • Gavin P., Devenish R.J., Prescott M. An approach for reducing unwanted oligomerisation of DsRed fusion proteins. Biochem. Biophys. Res. Commun. 298:2002;707-713.
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 707-713
    • Gavin, P.1    Devenish, R.J.2    Prescott, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.