메뉴 건너뛰기




Volumn 1457, Issue 1-2, 2000, Pages 81-93

A covalent tandem dimer of the mitochondrial ADP/ATP carrier is functional in vivo

Author keywords

ADP ATP carrier; Covalent tandem dimer; Saccharomyces cerevisiae; Subunit stoichiometry; Topography

Indexed keywords

ADENINE NUCLEOTIDE TRANSLOCASE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; DIMER; MONOMER;

EID: 0039742269     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(99)00115-2     Document Type: Article
Times cited : (43)

References (43)
  • 1
    • 0025899923 scopus 로고
    • Transmembrane topography of the mitochondrial phosphate carrier explored by peptide-specific antibodies and enzymatic digestion
    • Capobianco L., Brandolin G., Palmieri F. Transmembrane topography of the mitochondrial phosphate carrier explored by peptide-specific antibodies and enzymatic digestion. Biochemistry. 39:1991;4963-4969.
    • (1991) Biochemistry , vol.39 , pp. 4963-4969
    • Capobianco, L.1    Brandolin, G.2    Palmieri, F.3
  • 2
    • 0028798146 scopus 로고
    • The N- And C-termini of the tricarboxylate carrier are exposed to the cytoplasmic side of the inner mitochondrial membrane
    • Capobianco L., Bisaccia F., Michel A., Sluse F.E., Palmieri F. The N- and C-termini of the tricarboxylate carrier are exposed to the cytoplasmic side of the inner mitochondrial membrane. FEBS Lett. 357:1995;297-300.
    • (1995) FEBS Lett. , vol.357 , pp. 297-300
    • Capobianco, L.1    Bisaccia, F.2    Michel, A.3    Sluse, F.E.4    Palmieri, F.5
  • 3
    • 0023662148 scopus 로고
    • In the uncoupling protein from brown adipose tissue the C-terminus protrudes to the C-side of the membrane, as shown by tryptic cleavage
    • Eckerskorn C., Klingenberg M. In the uncoupling protein from brown adipose tissue the C-terminus protrudes to the C-side of the membrane, as shown by tryptic cleavage. FEBS Lett. 226:1987;166-170.
    • (1987) FEBS Lett. , vol.226 , pp. 166-170
    • Eckerskorn, C.1    Klingenberg, M.2
  • 5
    • 0024555951 scopus 로고
    • Orientation of the N-terminal region of the membrane bound ADP/ATP carrier explored by antipeptidases and arginine-specific endoproteases. Evidence that the accessibility of the N-terminal residues depends on the conformational state of the carrier
    • Brandolin G., Boulay F., Dalbon P., Vignais P.V. Orientation of the N-terminal region of the membrane bound ADP/ATP carrier explored by antipeptidases and arginine-specific endoproteases. Evidence that the accessibility of the N-terminal residues depends on the conformational state of the carrier. Biochemistry. 28:1989;1093-1100.
    • (1989) Biochemistry , vol.28 , pp. 1093-1100
    • Brandolin, G.1    Boulay, F.2    Dalbon, P.3    Vignais, P.V.4
  • 6
    • 0019316912 scopus 로고
    • Molecular mass and hydrodynamic parameters of the adenosine 5′-diphosphate-adenosine 5′-triphosphate carrier in Triton X-100
    • Hackenberg H., Klingenberg M. Molecular mass and hydrodynamic parameters of the adenosine 5′-diphosphate-adenosine 5′-triphosphate carrier in Triton X-100. Biochemistry. 19:1980;548-555.
    • (1980) Biochemistry , vol.19 , pp. 548-555
    • Hackenberg, H.1    Klingenberg, M.2
  • 7
    • 0020494167 scopus 로고
    • Small angle neutron scattering of the mitochondrial ADP/ATP carrier protein in detergent
    • Block M., Zaccaï G., Lauquin G.J.-M., Vignais P.V. Small angle neutron scattering of the mitochondrial ADP/ATP carrier protein in detergent. Biochem. Biophys. Res. Commun. 109:1982;471-477.
    • (1982) Biochem. Biophys. Res. Commun. , vol.109 , pp. 471-477
    • Block, M.1    Zaccaï, G.2    Lauquin, G.J.-M.3    Vignais, P.V.4
  • 8
    • 0017807928 scopus 로고
    • Isolation of ADP/ATP carrier as the carboxyatractylate protein complex from mitochondria
    • Klingenberg M., Riccio P., Aquila H. Isolation of ADP/ATP carrier as the carboxyatractylate protein complex from mitochondria. Biochim. Biophys. Acta. 503:1978;193-210.
    • (1978) Biochim. Biophys. Acta , vol.503 , pp. 193-210
    • Klingenberg, M.1    Riccio, P.2    Aquila, H.3
  • 9
    • 85052438250 scopus 로고
    • Molecular aspects of structure relationships in mitochondrial adenine nucleotide carrier
    • in: G. Bengha (Ed.) CRC Press, Boca Raton, FL
    • P.V. Vignais, M.R. Block, F. Boulay, G. Brandolin, G.J.-M. Lauquin, Molecular aspects of structure relationships in mitochondrial adenine nucleotide carrier, in: G. Bengha (Ed.), Structure and Properties of Cell Membranes, vol. II, CRC Press, Boca Raton, FL, 1985, pp. 139-179.
    • (1985) Structure and Properties of Cell Membranes , vol.2 , pp. 139-179
    • Vignais, P.V.1    Block, M.R.2    Boulay, F.3    Brandolin, G.4    Lauquin, G.J.-M.5
  • 10
    • 0028840853 scopus 로고
    • Translocation of loops regulates transport activity of mitochondrial ADP/ATP carrier as deduced from formation of a specific intermolecular disulfide bridge catalyzed by copper-o-phenanthroline
    • Majima E., Ikawa K., Takeda M., Hashimoto M., Shinohara Y., Terada H. Translocation of loops regulates transport activity of mitochondrial ADP/ATP carrier as deduced from formation of a specific intermolecular disulfide bridge catalyzed by copper-o-phenanthroline. J. Biol. Chem. 270:1995;29548-29554.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29548-29554
    • Majima, E.1    Ikawa, K.2    Takeda, M.3    Hashimoto, M.4    Shinohara, Y.5    Terada, H.6
  • 11
    • 0021748635 scopus 로고
    • Substrate-site interactions in the membrane-bound adenine-nucleotide carrier as disclosed by ADP and ATP analogs
    • Block M., Vignais P.V. Substrate-site interactions in the membrane-bound adenine-nucleotide carrier as disclosed by ADP and ATP analogs. Biochim. Biophys. Acta. 767:1984;369-376.
    • (1984) Biochim. Biophys. Acta , vol.767 , pp. 369-376
    • Block, M.1    Vignais, P.V.2
  • 12
    • 0020477022 scopus 로고
    • Exploration of the nucleotide binding sites of the isolated ADP/ATP carrier protein from Beef heart mitochondria. 1. Probing of the nucleotide sites by naphthoyl-ATP, a fluorescent nontransportable analogue of ATP
    • Dupont Y., Brandolin G., Vignais P.V. Exploration of the nucleotide binding sites of the isolated ADP/ATP carrier protein from Beef heart mitochondria. 1. Probing of the nucleotide sites by naphthoyl-ATP, a fluorescent nontransportable analogue of ATP. Biochemistry. 21:1982;6343-6347.
    • (1982) Biochemistry , vol.21 , pp. 6343-6347
    • Dupont, Y.1    Brandolin, G.2    Vignais, P.V.3
  • 13
    • 0020477031 scopus 로고
    • Exploration of the nucleotide binding sites of the isolated ADP/ATP carrier protein from Beef heart mitochondria. 2. Probing of the nucleotide sites by formicin triphosphate, a fluorescent transportable analogue of ATP
    • Brandolin G., Dupont Y., Vignais P.V. Exploration of the nucleotide binding sites of the isolated ADP/ATP carrier protein from Beef heart mitochondria. 2. Probing of the nucleotide sites by formicin triphosphate, a fluorescent transportable analogue of ATP. Biochemistry. 21:1982;6348-6353.
    • (1982) Biochemistry , vol.21 , pp. 6348-6353
    • Brandolin, G.1    Dupont, Y.2    Vignais, P.V.3
  • 14
    • 0025915949 scopus 로고
    • ADP/ATP translocator is essential only for anaerobic growth of yeast Saccharomyces cerevisiae
    • Drgon T., Sabová L., Nelson N., Kolarov J. ADP/ATP translocator is essential only for anaerobic growth of yeast Saccharomyces cerevisiae. FEBS Lett. 289:1991;159-162.
    • (1991) FEBS Lett. , vol.289 , pp. 159-162
    • Drgon, T.1    Sabová, L.2    Nelson, N.3    Kolarov, J.4
  • 16
    • 0027301486 scopus 로고
    • Biochemical characterisation of the isolated Anc2 adenine nucleotide carrier from Saccharomyces cerevisiae mitochondria
    • Brandolin G., Le Saux A., Trézéguet V., Vignais P.V., Lauquin G.J.-M. Biochemical characterisation of the isolated Anc2 adenine nucleotide carrier from Saccharomyces cerevisiae mitochondria. Biochem. Biophys. Res. Commun. 192:1993;143-150.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 143-150
    • Brandolin, G.1    Le Saux, A.2    Trézéguet, V.3    Vignais, P.V.4    Lauquin, G.J.-M.5
  • 18
    • 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
  • 19
    • 0016246225 scopus 로고
    • Partial purification of an atractyloside binding protein from mitochondria
    • Brandolin G., Meyer C., Defaye G., Vignais P.M., Vignais P.V. Partial purification of an atractyloside binding protein from mitochondria. FEBS Lett. 46:1974;149-153.
    • (1974) FEBS Lett. , vol.46 , pp. 149-153
    • Brandolin, G.1    Meyer, C.2    Defaye, G.3    Vignais, P.M.4    Vignais, P.V.5
  • 20
    • 0017717608 scopus 로고
    • Freezing of competent cells
    • Morrison A. Freezing of competent cells. J. Bacteriol. 132:1977;349.
    • (1977) J. Bacteriol. , vol.132 , pp. 349
    • Morrison, A.1
  • 21
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz D., St Jean R., Woods R.A., Schiestl R.H. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20:1992;1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, R.2    Woods, R.A.3    Schiestl, R.H.4
  • 22
    • 0019862344 scopus 로고
    • A rapid boiling method for the preparation of bacterial plasmids
    • Holmes D.S., Quigley M. A rapid boiling method for the preparation of bacterial plasmids. Anal. Biochem. 114:1981;193-197.
    • (1981) Anal. Biochem. , vol.114 , pp. 193-197
    • Holmes, D.S.1    Quigley, M.2
  • 24
    • 0020479807 scopus 로고
    • Import of proteins into mitochondria
    • Daum G., Böhni P., Schatz G. Import of proteins into mitochondria. J. Biol. Chem. 257:1982;13028-13033.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Böhni, P.2    Schatz, G.3
  • 25
    • 0030482902 scopus 로고    scopus 로고
    • Conformational changes of the yeast mitochondrial ADP/ATP carrier studied through its intrinsic fluorescence. 1. The tryptophanyl residues of the carrier can be mutated without impairing protein activity
    • Le Saux A., Roux P., Trézéguet V., Fiore C., Schwimmer C., Dianoux A.C., Vignais P.V., Brandolin G., Lauquin G.J.-M. Conformational changes of the yeast mitochondrial ADP/ATP carrier studied through its intrinsic fluorescence. 1. The tryptophanyl residues of the carrier can be mutated without impairing protein activity. Biochemistry. 35:1996;16116-16124.
    • (1996) Biochemistry , vol.35 , pp. 16116-16124
    • Le Saux, A.1    Roux, P.2    Trézéguet, V.3    Fiore, C.4    Schwimmer, C.5    Dianoux, A.C.6    Vignais, P.V.7    Brandolin, G.8    Lauquin, G.J.-M.9
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 277:1970;680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0025282180 scopus 로고
    • A third ADP/ATP translocator gene in yeast
    • Kolarov J., Kolarova N., Nelson N. A third ADP/ATP translocator gene in yeast. J. Biol. Chem. 265:1990;12711-12716.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12711-12716
    • Kolarov, J.1    Kolarova, N.2    Nelson, N.3
  • 28
    • 0025033857 scopus 로고
    • Structure-function studies of adenine nucleotide transport in mitochondria. I. Construction and genetic analysis of yeast mutants encoding the ADP/ATP carrier protein of mitochondria
    • Lawson J.E., Gawaz M., Klingenberg M., Douglas M.G. Structure-function studies of adenine nucleotide transport in mitochondria. I. Construction and genetic analysis of yeast mutants encoding the ADP/ATP carrier protein of mitochondria. J. Biol. Chem. 265:1990;14195-14201.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14195-14201
    • Lawson, J.E.1    Gawaz, M.2    Klingenberg, M.3    Douglas, M.G.4
  • 29
    • 0019888608 scopus 로고
    • Purification and reconstitution of functional lactose carrier from Escherichia coli
    • Newman M.J., Foster D.L., Wilson T.H., Kaback R.H. Purification and reconstitution of functional lactose carrier from Escherichia coli. J. Biol. Chem. 256:1981;11804-11808.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11804-11808
    • Newman, M.J.1    Foster, D.L.2    Wilson, T.H.3    Kaback, R.H.4
  • 30
    • 0025310534 scopus 로고
    • In vivo expression of the lacY gene in two segments leads to functional lac permease
    • Bibi E., Kaback R.H. In vivo expression of the lacY gene in two segments leads to functional lac permease. Proc. Natl. Acad. Sci. USA. 87:1990;4325-4329.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4325-4329
    • Bibi, E.1    Kaback, R.H.2
  • 31
    • 0030456167 scopus 로고    scopus 로고
    • Conformational changes of the yeast mitochondrial ADP/ATP carrier studied through its intrinsic fluorescence. 2. Assignment of tryptophanyl residues of the carrier to the responses to specific ligands
    • Roux P., Le Saux A., Trézéguet V., Fiore C., Schwimmer C., Dianoux A.C., Vignais P.V., Lauquin G.J.-M., Brandolin G. Conformational changes of the yeast mitochondrial ADP/ATP carrier studied through its intrinsic fluorescence. 2. Assignment of tryptophanyl residues of the carrier to the responses to specific ligands. Biochemistry. 35:1996;16125-16131.
    • (1996) Biochemistry , vol.35 , pp. 16125-16131
    • Roux, P.1    Le Saux, A.2    Trézéguet, V.3    Fiore, C.4    Schwimmer, C.5    Dianoux, A.C.6    Vignais, P.V.7    Lauquin, G.J.-M.8    Brandolin, G.9
  • 32
    • 0017114190 scopus 로고
    • Iodination of peripheral mitochondrial membrane proteins in correlation to the functional state of the ADP/ATP carrier
    • Brdiczka D., Schumacher D. Iodination of peripheral mitochondrial membrane proteins in correlation to the functional state of the ADP/ATP carrier. Biochem. Biophys. Res. Commun. 73:1976;823-832.
    • (1976) Biochem. Biophys. Res. Commun. , vol.73 , pp. 823-832
    • Brdiczka, D.1    Schumacher, D.2
  • 33
    • 0021770873 scopus 로고
    • Localization of the N-ethylmaleimide reactive cysteine in the beef heart mitochondria ADP/ATP carrier protein
    • Boulay F., Vignais P.V. Localization of the N-ethylmaleimide reactive cysteine in the beef heart mitochondria ADP/ATP carrier protein. Biochemistry. 23:1984;4807-4812.
    • (1984) Biochemistry , vol.23 , pp. 4807-4812
    • Boulay, F.1    Vignais, P.V.2
  • 34
    • 0022883823 scopus 로고
    • The transmembrane arrangement of the ADP/ATP carrier as elucidated by the lysine reagent pyridoxal-5-phosphate
    • Bogner W., Aquila H., Klingenberg M. The transmembrane arrangement of the ADP/ATP carrier as elucidated by the lysine reagent pyridoxal-5-phosphate. Eur. J. Biochem. 161:1986;611-620.
    • (1986) Eur. J. Biochem. , vol.161 , pp. 611-620
    • Bogner, W.1    Aquila, H.2    Klingenberg, M.3
  • 35
    • 0026718833 scopus 로고
    • Topography of the membrane-bound ADP/ATP carrier assessed by enzymatic proteolysis
    • Marty I., Brandolin G., Vignais P.V. Topography of the membrane-bound ADP/ATP carrier assessed by enzymatic proteolysis. Biochemistry. 31:1992;4058-4065.
    • (1992) Biochemistry , vol.31 , pp. 4058-4065
    • Marty, I.1    Brandolin, G.2    Vignais, P.V.3
  • 37
    • 0029743660 scopus 로고    scopus 로고
    • Two physically distinct pores in the dimeric ClC-0 chloride channel
    • Ludewig U., Pusch M., Jentsch T.J. Two physically distinct pores in the dimeric ClC-0 chloride channel. Nature. 383:1996;340-343.
    • (1996) Nature , vol.383 , pp. 340-343
    • Ludewig, U.1    Pusch, M.2    Jentsch, T.J.3
  • 38
    • 0032486483 scopus 로고    scopus 로고
    • The phosphate carrier from yeast mitochondria. Dimerization is a prerequisite for function
    • Schroers A., Burkovski A., Wohlrab H., Krämer R. The phosphate carrier from yeast mitochondria. Dimerization is a prerequisite for function. J. Biol. Chem. 273:1998;14269-14276.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14269-14276
    • Schroers, A.1    Burkovski, A.2    Wohlrab, H.3    Krämer, R.4
  • 39
    • 0014214363 scopus 로고
    • Biochemical genetics of oxidative phosphorylation
    • Kovác L., Lachowicz T.M., Slonimski P.P. Biochemical genetics of oxidative phosphorylation. Science. 158:1967;1564-1567.
    • (1967) Science , vol.158 , pp. 1564-1567
    • Kovác, L.1    Lachowicz, T.M.2    Slonimski, P.P.3
  • 40
    • 0026663246 scopus 로고
    • Evidence for cooperative interactions in potassium channel gating
    • Tytgat J., Hess P. Evidence for cooperative interactions in potassium channel gating. Science. 359:1992;420-423.
    • (1992) Science , vol.359 , pp. 420-423
    • Tytgat, J.1    Hess, P.2
  • 41
    • 0020475449 scopus 로고
    • A simple method for displaying the hydrophobic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydrophobic character of a protein. J. Mol. Biol. 157:1982;105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 42
    • 0020473533 scopus 로고
    • Internal sequence repeats and the path of polypeptide in mitochondrial ADP/ATP translocase
    • Saraste M., Walker J.E. Internal sequence repeats and the path of polypeptide in mitochondrial ADP/ATP translocase. FEBS Lett. 144:1982;250-254.
    • (1982) FEBS Lett. , vol.144 , pp. 250-254
    • Saraste, M.1    Walker, J.E.2
  • 43
    • 0030456168 scopus 로고    scopus 로고
    • Probing the role of positive residues in the ADP/ATP carrier from yeast. The effect of six arginine mutations on oxidative phosphorylation and AAC expression
    • Müller V., Basset G., Nelson D.R., Klingenberg M. Probing the role of positive residues in the ADP/ATP carrier from yeast. The effect of six arginine mutations on oxidative phosphorylation and AAC expression. Biochemistry. 35:1996;16132-16143.
    • (1996) Biochemistry , vol.35 , pp. 16132-16143
    • Müller, V.1    Basset, G.2    Nelson, D.R.3    Klingenberg, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.