메뉴 건너뛰기




Volumn 189, Issue 19, 2007, Pages 7089-7097

Topology of AspT, the aspartate:alanine antiporter of Tetragenococcus halophilus, determined by site-directed fluorescence labeling

Author keywords

[No Author keywords available]

Indexed keywords

[2 (TRIMETHYLAMMONIUM)ETHYL]METHANETHIOSULFONATE BROMIDE; ALANINE; ANTIPORTER; ARGININE; ASPARTATE BETA DECARBOXYLASE; ASPARTIC ACID; CARBON DIOXIDE; CARBOXYLYASE; CYSTEINE; HISTIDINE; MALEIMIDE; PROTEIN ASPT; SULFONIC ACID DERIVATIVE; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 34948849760     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00088-07     Document Type: Article
Times cited : (17)

References (47)
  • 1
    • 0030063772 scopus 로고    scopus 로고
    • Exchange of aspartate and alanine. Mechanism for development of a proton-motive force in bacteria
    • Abe, K., H. Hayashi, and P. C. Maloney. 1996. Exchange of aspartate and alanine. Mechanism for development of a proton-motive force in bacteria. J. Biol. Chem. 271:3079-3084.
    • (1996) J. Biol. Chem , vol.271 , pp. 3079-3084
    • Abe, K.1    Hayashi, H.2    Maloney, P.C.3
  • 2
    • 0036098106 scopus 로고    scopus 로고
    • Plasmid-encoded asp operon confers a proton motive metabolic cycle catalyzed by an aspartate-alanine exchange reaction
    • Abe, K., F. Ohnishi, K. Yagi, T. Nakajima, T. Higuchi, M. Sano, M. Machida, R. I. Sarker, and P. C. Maloney. 2002. Plasmid-encoded asp operon confers a proton motive metabolic cycle catalyzed by an aspartate-alanine exchange reaction. J. Bacteriol. 184:2906-2913.
    • (2002) J. Bacteriol , vol.184 , pp. 2906-2913
    • Abe, K.1    Ohnishi, F.2    Yagi, K.3    Nakajima, T.4    Higuchi, T.5    Sano, M.6    Machida, M.7    Sarker, R.I.8    Maloney, P.C.9
  • 3
    • 0029917173 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression in Escherichia coli of OxlT, the oxalate:formate exchange protein of Oxalobacter formigenes
    • Abe, K., Z. S. Ruan, and P. C. Maloney. 1996. Cloning, sequencing, and expression in Escherichia coli of OxlT, the oxalate:formate exchange protein of Oxalobacter formigenes. J. Biol. Chem. 271:6789-6793.
    • (1996) J. Biol. Chem , vol.271 , pp. 6789-6793
    • Abe, K.1    Ruan, Z.S.2    Maloney, P.C.3
  • 4
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutants
    • Akabas, M. H., D. A. Stauffer, M. Xu, and A. Karlin. 1992. Acetylcholine receptor channel structure probed in cysteine-substitution mutants. Science 258:307-310.
    • (1992) Science , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 7
    • 0022827885 scopus 로고
    • Bacterial anion exchange. Use of osmolytes during solubilization and reconstitution of phosphate-linked antiport from Streptococcus lactis
    • Ambudkar, S. V., and P. C. Maloney. 1986. Bacterial anion exchange. Use of osmolytes during solubilization and reconstitution of phosphate-linked antiport from Streptococcus lactis. J. Biol. Chem. 261:10079-10086.
    • (1986) J. Biol. Chem , vol.261 , pp. 10079-10086
    • Ambudkar, S.V.1    Maloney, P.C.2
  • 8
    • 0024961965 scopus 로고
    • Oxalate:formate exchange. The basis for energy coupling in Oxalobacter
    • Anantharam, V., M. J. Allison, and P. C. Maloney. 1989. Oxalate:formate exchange. The basis for energy coupling in Oxalobacter. J. Biol. Chem. 264:7244-7250.
    • (1989) J. Biol. Chem , vol.264 , pp. 7244-7250
    • Anantharam, V.1    Allison, M.J.2    Maloney, P.C.3
  • 9
    • 0035853296 scopus 로고    scopus 로고
    • Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains
    • Anantharaman, V., E. V. Koonin, and L. Aravind. 2001. Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains. J. Mol. Biol. 307:1271-1292.
    • (2001) J. Mol. Biol , vol.307 , pp. 1271-1292
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 10
    • 0035166973 scopus 로고    scopus 로고
    • Apweiler, R., T. K. Attwood, A. Bairoch, A. Bateman, E. Birney, M. Biswas, P. Bucher, L. Cerutti, F. Corpet, M. D. Croning, R. Durbin, L. Falquet, W. Fleischmann, J. Gouzy, H. Hermjakob, N. Hulo, I. Jonassen, D. Kahn, A. Kanapin, Y. Karavidopoulou, R. Lopez, B. Marx, N. J. Mulder, T. M. Oinn, M. Pagni, F. Servant, C. J. Sigrist, and E. M. Zdobnov. 2001. The InterPro database, an integrated documentation resource for protein families, domains and functional sites. Nucleic Acids Res. 29:37-40.
    • Apweiler, R., T. K. Attwood, A. Bairoch, A. Bateman, E. Birney, M. Biswas, P. Bucher, L. Cerutti, F. Corpet, M. D. Croning, R. Durbin, L. Falquet, W. Fleischmann, J. Gouzy, H. Hermjakob, N. Hulo, I. Jonassen, D. Kahn, A. Kanapin, Y. Karavidopoulou, R. Lopez, B. Marx, N. J. Mulder, T. M. Oinn, M. Pagni, F. Servant, C. J. Sigrist, and E. M. Zdobnov. 2001. The InterPro database, an integrated documentation resource for protein families, domains and functional sites. Nucleic Acids Res. 29:37-40.
  • 11
    • 33749075765 scopus 로고    scopus 로고
    • Barabote, R. D., D. G. Tamang, S. N. Abeywardena, N. S. Fallah, J. Y. Fu, J. K. Lio, P. Mirhosseini, R. Pezeshk, S. Podell, M. L. Salampessy, M. D. Thever, and M. H. Saier, Jr. 2006. Extra domains in secondary transport carriers and channel proteins. Biochim. Biophys. Acta 1758:1557-1579.
    • Barabote, R. D., D. G. Tamang, S. N. Abeywardena, N. S. Fallah, J. Y. Fu, J. K. Lio, P. Mirhosseini, R. Pezeshk, S. Podell, M. L. Salampessy, M. D. Thever, and M. H. Saier, Jr. 2006. Extra domains in secondary transport carriers and channel proteins. Biochim. Biophys. Acta 1758:1557-1579.
  • 12
    • 19444377006 scopus 로고    scopus 로고
    • Transmembrane protein topology mapping by the substituted cysteine accessibility method (SCAM(TM)): Application to lipid-specific membrane protein topogenesis
    • Bogdanov, M., W. Zhang, J. Xie, and W. Dowhan. 2005. Transmembrane protein topology mapping by the substituted cysteine accessibility method (SCAM(TM)): application to lipid-specific membrane protein topogenesis. Methods 36:148-171.
    • (2005) Methods , vol.36 , pp. 148-171
    • Bogdanov, M.1    Zhang, W.2    Xie, J.3    Dowhan, W.4
  • 14
    • 0026315381 scopus 로고
    • In vivo topological analysis of Ste2, a yeast plasma membrane protein, by using beta-lactamase gene fusions
    • Cartwright, C. P., and D. J. Tipper. 1991. In vivo topological analysis of Ste2, a yeast plasma membrane protein, by using beta-lactamase gene fusions. Mol. Cell. Biol. 11:2620-2628.
    • (1991) Mol. Cell. Biol , vol.11 , pp. 2620-2628
    • Cartwright, C.P.1    Tipper, D.J.2
  • 15
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • Engelman, D. M., T. A. Steitz, and A. Goldman. 1986. Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys. Biophys. Chem. 15:321-353.
    • (1986) Annu. Rev. Biophys. Biophys. Chem , vol.15 , pp. 321-353
    • Engelman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 16
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • Frishman, D., and P. Argos. 1995. Knowledge-based protein secondary structure assignment. Proteins 23:566-579.
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 17
    • 0031027519 scopus 로고    scopus 로고
    • Evaluation of secondary structure of OxlT, the oxalate transporter of Oxalobacter formigenes, by circular dichroism spectroscopy
    • Fu, D., and P. C. Maloney. 1997. Evaluation of secondary structure of OxlT, the oxalate transporter of Oxalobacter formigenes, by circular dichroism spectroscopy. J. Biol. Chem. 272:2129-2135.
    • (1997) J. Biol. Chem , vol.272 , pp. 2129-2135
    • Fu, D.1    Maloney, P.C.2
  • 18
    • 0032504246 scopus 로고    scopus 로고
    • Structure-function relationships in OxlT, the oxalate/formate transporter of Oxalobacter formigenes. Topological features of transmembrane helix 11 as visualized by site-directed fluorescent labeling
    • Fu, D., and P. C. Maloney. 1998. Structure-function relationships in OxlT, the oxalate/formate transporter of Oxalobacter formigenes. Topological features of transmembrane helix 11 as visualized by site-directed fluorescent labeling. J. Biol. Chem. 273:17962-17967.
    • (1998) J. Biol. Chem , vol.273 , pp. 17962-17967
    • Fu, D.1    Maloney, P.C.2
  • 19
    • 0035937821 scopus 로고    scopus 로고
    • Structure/function relationships in OxlT, the oxalate-formate transporter of Oxalobacter formigenes. Assignment of transmembrane helix 11 to the translocation pathway
    • Fu, D., R. I. Sarker, K. Abe, E. Bolton, and P. C. Maloney. 2001. Structure/function relationships in OxlT, the oxalate-formate transporter of Oxalobacter formigenes. Assignment of transmembrane helix 11 to the translocation pathway. J. Biol. Chem. 276:8753-8760.
    • (2001) J. Biol. Chem , vol.276 , pp. 8753-8760
    • Fu, D.1    Sarker, R.I.2    Abe, K.3    Bolton, E.4    Maloney, P.C.5
  • 21
    • 0032169137 scopus 로고    scopus 로고
    • Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology
    • Grunewald, M., A. Bendahan, and B. I. Kanner. 1998. Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology. Neuron 21:623-632.
    • (1998) Neuron , vol.21 , pp. 623-632
    • Grunewald, M.1    Bendahan, A.2    Kanner, B.I.3
  • 22
    • 0029584356 scopus 로고
    • Plasmids with a kanamycin-resistance gene for site-directed mutagenesis using the oligodeoxyribonucleotide-directed dual amber method
    • Hashimoto-Gotoh, T., K. Yasojima, and A. Tsujimura. 1995. Plasmids with a kanamycin-resistance gene for site-directed mutagenesis using the oligodeoxyribonucleotide-directed dual amber method. Gene 167:333-334.
    • (1995) Gene , vol.167 , pp. 333-334
    • Hashimoto-Gotoh, T.1    Yasojima, K.2    Tsujimura, A.3
  • 23
    • 0029159445 scopus 로고
    • Molecular and enzymatic properties of an aspartic proteinase from Rhizopus hangchow
    • Ichishima, E., M. Ojima, Y. Yamagata, S. Hanzawa, and T. Nakamura. 1995. Molecular and enzymatic properties of an aspartic proteinase from Rhizopus hangchow. Phytochemistry 38:27-30.
    • (1995) Phytochemistry , vol.38 , pp. 27-30
    • Ichishima, E.1    Ojima, M.2    Yamagata, Y.3    Hanzawa, S.4    Nakamura, T.5
  • 26
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D. T. 1999. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292:195-202.
    • (1999) J. Mol. Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 28
    • 0032321487 scopus 로고    scopus 로고
    • Substituted-cysteine accessibility method
    • Karlin, A., and M. H. Akabas. 1998. Substituted-cysteine accessibility method. Methods Enzymol. 293:123-145.
    • (1998) Methods Enzymol , vol.293 , pp. 123-145
    • Karlin, A.1    Akabas, M.H.2
  • 30
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 31
    • 0028928984 scopus 로고
    • Membrane topology of a cysteine-less mutant of human P-glycoprotein
    • Loo, T. W., and D. M. Clarke. 1995. Membrane topology of a cysteine-less mutant of human P-glycoprotein. J. Biol. Chem. 270:843-848.
    • (1995) J. Biol. Chem , vol.270 , pp. 843-848
    • Loo, T.W.1    Clarke, D.M.2
  • 32
    • 0028534903 scopus 로고
    • Bacterial anion exchange: Reductionist and integrative approaches to membrane biology
    • Maloney, P. C., R. T. Yan, and K. Abe. 1994. Bacterial anion exchange: reductionist and integrative approaches to membrane biology. J. Exp. Biol. 196:471-482.
    • (1994) J. Exp. Biol , vol.196 , pp. 471-482
    • Maloney, P.C.1    Yan, R.T.2    Abe, K.3
  • 33
    • 0023028051 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil, C., and J. Beckwith. 1986. A genetic approach to analyzing membrane protein topology. Science 233:1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 34
    • 12844256463 scopus 로고    scopus 로고
    • Membrane topology of the electrogenic aspartate-alanine antiporter AspT of Tetragenococcus halophilus
    • Nanatani, K., F. Ohonishi, H. Yoneyama, T. Nakajima, and K. Abe. 2005. Membrane topology of the electrogenic aspartate-alanine antiporter AspT of Tetragenococcus halophilus. Biochem. Biophys. Res. Commun. 328:20-26.
    • (2005) Biochem. Biophys. Res. Commun , vol.328 , pp. 20-26
    • Nanatani, K.1    Ohonishi, F.2    Yoneyama, H.3    Nakajima, T.4    Abe, K.5
  • 35
    • 0034465184 scopus 로고    scopus 로고
    • An automatic homology modeling method consisting of database searches and simulated annealing
    • Ogata, K., and H. Umeyama. 2000. An automatic homology modeling method consisting of database searches and simulated annealing. J. Mol. Graph. Model. 18:258-272.
    • (2000) J. Mol. Graph. Model , vol.18 , pp. 258-272
    • Ogata, K.1    Umeyama, H.2
  • 37
    • 0026731206 scopus 로고
    • Identification, purification, and reconstitution of OxlT, the oxalate:formate antiport protein of Oxalobacter formigenes
    • Ruan, Z. S., V. Anantharam, I. T. Crawford, S. V. Ambudkar, S. Y. Rhee, M. J. Allison, and P. C. Maloney. 1992. Identification, purification, and reconstitution of OxlT, the oxalate:formate antiport protein of Oxalobacter formigenes. J. Biol. Chem. 267:10537-10543.
    • (1992) J. Biol. Chem , vol.267 , pp. 10537-10543
    • Ruan, Z.S.1    Anantharam, V.2    Crawford, I.T.3    Ambudkar, S.V.4    Rhee, S.Y.5    Allison, M.J.6    Maloney, P.C.7
  • 38
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov, I. N., and P. E. Bourne. 1998. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11:739-747.
    • (1998) Protein Eng , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 39
    • 33746139292 scopus 로고    scopus 로고
    • FAMS complex: A fully automated homology modeling system for protein complex structures
    • Takeda-Shitaka, M., G. Terashi, C. Chiba, D. Takaya, and H. Umeyama. 2006. FAMS complex: a fully automated homology modeling system for protein complex structures. Med. Chem. 2:191-201.
    • (2006) Med. Chem , vol.2 , pp. 191-201
    • Takeda-Shitaka, M.1    Terashi, G.2    Chiba, C.3    Takaya, D.4    Umeyama, H.5
  • 41
    • 0142168992 scopus 로고    scopus 로고
    • + antiport: Complete cysteine-scanning mutagenesis and the protein engineering approach
    • + antiport: complete cysteine-scanning mutagenesis and the protein engineering approach. Curr. Opin. Chem. Biol. 7:570-579.
    • (2003) Curr. Opin. Chem. Biol , vol.7 , pp. 570-579
    • Tamura, N.1    Konishi, S.2    Yamaguchi, A.3
  • 42
    • 0025110961 scopus 로고
    • A rapid method for reconstitution of bacterial membrane proteins
    • Varadhachary, A., and P. C. Maloney. 1990. A rapid method for reconstitution of bacterial membrane proteins. Mol. Microbiol. 4:1407-1411.
    • (1990) Mol. Microbiol , vol.4 , pp. 1407-1411
    • Varadhachary, A.1    Maloney, P.C.2
  • 43
    • 33748651219 scopus 로고    scopus 로고
    • Analysis of substrate-binding elements in OxlT, the oxalate:formate antiporter of Oxalobacter formigenes
    • Wang, X., R. I. Sarker, and P. C. Maloney. 2006. Analysis of substrate-binding elements in OxlT, the oxalate:formate antiporter of Oxalobacter formigenes. Biochemistry 45:10344-10350.
    • (2006) Biochemistry , vol.45 , pp. 10344-10350
    • Wang, X.1    Sarker, R.I.2    Maloney, P.C.3
  • 44
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J. T., C. S. Wu, and H. M. Martinez. 1986. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130:208-269.
    • (1986) Methods Enzymol , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.2    Martinez, H.M.3
  • 45
    • 0035089130 scopus 로고    scopus 로고
    • Topology of OxlT, the oxalate transporter of Oxalobacter formigenes, determined by site-directed fluorescence labeling
    • Ye, L., Z. Jia, T. Jung, and P. C. Maloney. 2001. Topology of OxlT, the oxalate transporter of Oxalobacter formigenes, determined by site-directed fluorescence labeling. J. Bacteriol. 183:2490-2496.
    • (2001) J. Bacteriol , vol.183 , pp. 2490-2496
    • Ye, L.1    Jia, Z.2    Jung, T.3    Maloney, P.C.4
  • 46
    • 0037036449 scopus 로고    scopus 로고
    • Structure/function relationships in OxlT, the oxalate/formate antiporter of Oxalobacter formigenes: Assignment of transmembrane helix 2 to the translocation pathway
    • Ye, L., and P. C. Maloney. 2002. Structure/function relationships in OxlT, the oxalate/formate antiporter of Oxalobacter formigenes: assignment of transmembrane helix 2 to the translocation pathway. J. Biol. Chem. 277:20372-20378.
    • (2002) J. Biol. Chem , vol.277 , pp. 20372-20378
    • Ye, L.1    Maloney, P.C.2
  • 47
    • 33947098546 scopus 로고    scopus 로고
    • Topology of transmembrane proteins by scanning cysteine accessibility mutagenesis methodology
    • Zhu, Q., and J. R. Casey. 2007. Topology of transmembrane proteins by scanning cysteine accessibility mutagenesis methodology. Methods 41:439-450.
    • (2007) Methods , vol.41 , pp. 439-450
    • Zhu, Q.1    Casey, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.