메뉴 건너뛰기




Volumn 447, Issue 1, 2012, Pages 35-42

Alanine scanning mutagenesis of a high-affinity nitrate transporter highlights the requirement for glycine and asparagine residues in the two nitrate signature motifs

Author keywords

Alanine scanning; Helix packing; Major facilitator superfamily (MFS); Nitrate transporter; Structural model

Indexed keywords

ALANINE; ARGININE; ASPARAGINE; GLYCINE; NITRATE; NITRATE TRANSPORTER; NITRATE TRANSPORTER NRTA; NITRATE TRANSPORTER NS1; NITRATE TRANSPORTER NS2; UNCLASSIFIED DRUG;

EID: 84866399105     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20120631     Document Type: Article
Times cited : (11)

References (48)
  • 1
    • 42249089715 scopus 로고    scopus 로고
    • Nitrate assimilation in Chlamydomonas
    • Fernandez, E. and Galvan, A. (2008) Nitrate assimilation in Chlamydomonas. Eukaryot. Cell 7, 555-559
    • (2008) Eukaryot. Cell , vol.7 , pp. 555-559
    • Fernandez, E.1    Galvan, A.2
  • 3
    • 0034775280 scopus 로고    scopus 로고
    • Ammonia-oxidizing bacteria: A model for molecular microbial ecology
    • Kowalchuk, G. A. and Stephen, J. R. (2001) Ammonia-oxidizing bacteria: a model for molecular microbial ecology. Ann. Rev. Microbiol. 55, 485-529
    • (2001) Ann. Rev. Microbiol. , vol.55 , pp. 485-529
    • Kowalchuk, G.A.1    Stephen, J.R.2
  • 5
    • 67649876309 scopus 로고    scopus 로고
    • Food sources of nitrates and nitrites: The physiologic context for potential health benefits
    • Hord, N. G., Tang, Y. and Bryan, N. S. (2009) Food sources of nitrates and nitrites: the physiologic context for potential health benefits. Am. J. Clin. Nutr. 90, 1-10
    • (2009) Am. J. Clin. Nutr. , vol.90 , pp. 1-10
    • Hord, N.G.1    Tang, Y.2    Bryan, N.S.3
  • 6
    • 33746795832 scopus 로고    scopus 로고
    • Ecological and toxicological effects of inorganic nitrogen pollution in aquatic ecosystems: A global assessment
    • Camargo, J. A. and Alonso, A. (2006) Ecological and toxicological effects of inorganic nitrogen pollution in aquatic ecosystems: a global assessment. Environ. Int. 32, 831-849
    • (2006) Environ. Int. , vol.32 , pp. 831-849
    • Camargo, J.A.1    Alonso, A.2
  • 8
    • 33745615124 scopus 로고    scopus 로고
    • Atomic structure of a nitrate-binding protein crucial for photosynthetic productivity
    • Koropatkin, N. M., Pakrasi, H. B. and Smith, T. J. (2006) Atomic structure of a nitrate-binding protein crucial for photosynthetic productivity. Proc. Natl. Acad. Sci. U.S.A. 103, 9820-9825
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 9820-9825
    • Koropatkin, N.M.1    Pakrasi, H.B.2    Smith, T.J.3
  • 9
    • 34248193815 scopus 로고    scopus 로고
    • Nitrate transporters and peptide transporters
    • Tsay, Y. F., Chiu, C. C., Tsai, C. B., Ho, C. H. and Hsu, P. K. (2007) Nitrate transporters and peptide transporters. FEBS Lett. 581, 2290-2300
    • (2007) FEBS Lett. , vol.581 , pp. 2290-2300
    • Tsay, Y.F.1    Chiu, C.C.2    Tsai, C.B.3    Ho, C.H.4    Hsu, P.K.5
  • 12
    • 0030579205 scopus 로고    scopus 로고
    • Molecular cloning of higher plant homologues of the high-affinity nitrate transporters of Chlamydomonas reinhardtii and Aspergillus nidulans
    • Trueman, L. J., Richardson, A. and Forde, B. G. (1996) Molecular cloning of higher plant homologues of the high-affinity nitrate transporters of Chlamydomonas reinhardtii and Aspergillus nidulans. Gene 175, 223-231
    • (1996) Gene , vol.175 , pp. 223-231
    • Trueman, L.J.1    Richardson, A.2    Forde, B.G.3
  • 13
    • 0034194384 scopus 로고    scopus 로고
    • Nitrate transporters in plants: Structure, function and regulation
    • Forde, B. G. (2000) Nitrate transporters in plants: structure, function and regulation. Biochim. Biophys. Acta 1465, 219-235
    • (2000) Biochim. Biophys. Acta , vol.1465 , pp. 219-235
    • Forde, B.G.1
  • 15
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J., Smirnova, I., Kasho, V., Verner, G., Kaback, H. R. and Iwata, S. (2003) Structure and mechanism of the lactose permease of Escherichia coli. Science 301, 610-615
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 16
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Huang, Y., Lemieux, M. J., Song, J., Auer, M. and Wang, D. N. (2003) Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301, 616-620
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 17
    • 33646445156 scopus 로고    scopus 로고
    • Structure of the multidrug transporter EmrD from Escherichia coli
    • Yin, Y., He, X., Szewczyk, P., Nguyen, T. and Chang, G. (2006) Structure of the multidrug transporter EmrD from Escherichia coli. Science 312, 741-744
    • (2006) Science , vol.312 , pp. 741-744
    • Yin, Y.1    He, X.2    Szewczyk, P.3    Nguyen, T.4    Chang, G.5
  • 18
    • 77958010505 scopus 로고    scopus 로고
    • Structure of a fucose transporter in an outward-open conformation
    • Dang, S., Sun, L., Huang, Y., Lu, F., Liu, Y., Gong, H., Wang, J. and Yan, N. (2010) Structure of a fucose transporter in an outward-open conformation. Nature 467, 734-738
    • (2010) Nature , vol.467 , pp. 734-738
    • Dang, S.1    Sun, L.2    Huang, Y.3    Lu, F.4    Liu, Y.5    Gong, H.6    Wang, J.7    Yan, N.8
  • 20
    • 10644282958 scopus 로고    scopus 로고
    • Two perfectly conserved arginine residues are required for substrate binding in a high-affinity nitrate transporter
    • Unkles, S. E., Rouch, D. A., Wang, Y., Siddiqi, M. Y., Glass, A. D. and Kinghorn, J. R. (2004) Two perfectly conserved arginine residues are required for substrate binding in a high-affinity nitrate transporter. Proc. Natl. Acad. Sci. U.S.A. 101, 17549-17554
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 17549-17554
    • Unkles, S.E.1    Rouch, D.A.2    Wang, Y.3    Siddiqi, M.Y.4    Glass, A.D.5    Kinghorn, J.R.6
  • 21
    • 58249087122 scopus 로고    scopus 로고
    • A single channel for nitrate uptake, nitrite export and nitrite uptake by Escherichia coli NarU and a role for NirC in nitrite export and uptake
    • Jia, W., Tovell, N., Clegg, S., Trimmer, M. and Cole, J. (2009) A single channel for nitrate uptake, nitrite export and nitrite uptake by Escherichia coli NarU and a role for NirC in nitrite export and uptake. Biochem. J. 417, 297-304
    • (2009) Biochem. J. , vol.417 , pp. 297-304
    • Jia, W.1    Tovell, N.2    Clegg, S.3    Trimmer, M.4    Cole, J.5
  • 22
    • 0001350074 scopus 로고
    • Aspergillus nidulans
    • King, R. C., ed., Plenum Press, New York
    • Clutterbuck, A. J. (1974) Aspergillus nidulans. In Handbook of Genetics (vol. 1) (King, R. C., ed.), pp. 447-510, Plenum Press, New York
    • (1974) Handbook of Genetics , vol.1 , pp. 447-510
    • Clutterbuck, A.J.1
  • 23
    • 0014011862 scopus 로고
    • The induction and repression of nitrate reductase in the fungus Aspergillus nidulans
    • Cove, D. J. (1966) The induction and repression of nitrate reductase in the fungus Aspergillus nidulans. Biochim. Biophys. Acta 113, 51-56
    • (1966) Biochim. Biophys. Acta , vol.113 , pp. 51-56
    • Cove, D.J.1
  • 24
    • 0035890137 scopus 로고    scopus 로고
    • Apparent genetic redundancy facilitates ecological plasticity for nitrate transport
    • Unkles, S. E., Zhou, D., Siddiqi, M. Y., Kinghorn, J. R. and Glass, A. D. (2001) Apparent genetic redundancy facilitates ecological plasticity for nitrate transport. EMBO J. 20, 6246-6255
    • (2001) EMBO J. , vol.20 , pp. 6246-6255
    • Unkles, S.E.1    Zhou, D.2    Siddiqi, M.Y.3    Kinghorn, J.R.4    Glass, A.D.5
  • 25
    • 0001943739 scopus 로고
    • Fungal transformation
    • Bos, C., ed., Wiley Press, London
    • Riach, M. and Kinghorn, J. R. (1995) Fungal transformation. In Fungal Genetics (Bos, C., ed.), pp. 209-234, Wiley Press, London
    • (1995) Fungal Genetics , pp. 209-234
    • Riach, M.1    Kinghorn, J.R.2
  • 26
    • 0031579372 scopus 로고    scopus 로고
    • Splicing by overlap extension by PCR using asymmetric amplification: An improved technique for the generation of hybrid proteins of immunological interest
    • Warrens, A. N., Jones, M. D. and Lechler, R. I. (1997) Splicing by overlap extension by PCR using asymmetric amplification: an improved technique for the generation of hybrid proteins of immunological interest. Gene 186, 29-35
    • (1997) Gene , vol.186 , pp. 29-35
    • Warrens, A.N.1    Jones, M.D.2    Lechler, R.I.3
  • 27
    • 0025772724 scopus 로고
    • Identification of an epitope on the P and v proteins of simian virus 5 that distinguishes between two isolates with different biological characteristics
    • Southern, J. A., Young, D. F., Heaney, F., Baumgärtner, W. K. and Randall, R. E. (1991) Identification of an epitope on the P and V proteins of simian virus 5 that distinguishes between two isolates with different biological characteristics. J. Gen. Virol. 72, 1551-1557
    • (1991) J. Gen. Virol. , vol.72 , pp. 1551-1557
    • Southern, J.A.1    Young, D.F.2    Heaney, F.3    Baumgärtner, W.K.4    Randall, R.E.5
  • 28
    • 45949107473 scopus 로고    scopus 로고
    • Recent developments in the MAFFT multiple sequence alignment program
    • Katoh, K. and Toh, H. (2008) Recent developments in the MAFFT multiple sequence alignment program. Briefings Bioinf. 9, 286-298
    • (2008) Briefings Bioinf. , vol.9 , pp. 286-298
    • Katoh, K.1    Toh, H.2
  • 29
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2: A multiple sequence alignment editor and analysis workbench
    • Waterhouse, A. M., Procter, J. B., Martin, D. M. A, Clamp, M. and Barton, G. J. (2009) Jalview Version 2: a multiple sequence alignment editor and analysis workbench. Bioinformatics 25, 1189-1191
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.A.3    Clamp, M.4    Barton, G.J.5
  • 30
    • 0020593562 scopus 로고
    • Nitrate uptake in Aspergillus nidulans and involvement of the third gene of the nitrate assimilation gene cluster
    • Brownlee, A. G. and Arst, Jr, H. N. (1983) Nitrate uptake in Aspergillus nidulans and involvement of the third gene of the nitrate assimilation gene cluster. J. Bacteriol. 155, 1138-1146
    • (1983) J. Bacteriol. , vol.155 , pp. 1138-1146
    • Brownlee, A.G.1    Arst Jr., H.N.2
  • 31
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: A case study using the Phyre server
    • Kelley, L. A. and Sternberg, M. J. E. (2009) Protein structure prediction on the web: a case study using the Phyre server. Nat. Protoc. 4, 363-371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 32
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy, A., Kucukural, A. and Zhang, Y. (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat. Protoc. 5, 725-738
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 33
    • 34447256364 scopus 로고    scopus 로고
    • Conformational change in an MFS protein: MD simulations of LacY
    • Holyoake, J. and Sansom, M. S. (2007) Conformational change in an MFS protein: MD simulations of LacY. Structure 15, 873-884
    • (2007) Structure , vol.15 , pp. 873-884
    • Holyoake, J.1    Sansom, M.S.2
  • 34
    • 58949104204 scopus 로고    scopus 로고
    • Helix dynamics in a membrane transport protein: Comparative simulations of the glycerol-3-phosphate transporter and its constituent helices
    • D'Rozario, R. S. and Sansom, M. S. (2008) Helix dynamics in a membrane transport protein: comparative simulations of the glycerol-3-phosphate transporter and its constituent helices. Mol. Membr. Biol. 25, 571-583
    • (2008) Mol. Membr. Biol. , vol.25 , pp. 571-583
    • D'Rozario, R.S.1    Sansom, M.S.2
  • 36
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix-helix association
    • Russ, W. P. and Engelman, D. M. (2000) The GxxxG motif: a framework for transmembrane helix-helix association. J. Mol. Biol. 296, 911-919
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.A.1    Engelman, D.M.2
  • 37
    • 0037076540 scopus 로고    scopus 로고
    • GXXXG and AXXXA: Common α-helical interaction motifs in proteins, particularly in extremophiles
    • Kleiger, G., Grothe, R., Mallick, P. and Eisenberg, D. (2002) GXXXG and AXXXA: common α-helical interaction motifs in proteins, particularly in extremophiles. Biochemistry 41, 5990-5997
    • (2002) Biochemistry , vol.41 , pp. 5990-5997
    • Kleiger, G.1    Grothe, R.2    Mallick, P.3    Eisenberg, D.4
  • 38
    • 26444611461 scopus 로고    scopus 로고
    • Transmembrane glycine zippers: Physiological and pathological roles in membrane proteins
    • Kim, S., Jeon, T. J., Oberai, A., Yang, D., Schmidt, J. J. and Bowie, J. U. (2005) Transmembrane glycine zippers: physiological and pathological roles in membrane proteins. Proc. Natl. Acad. Sci. U.S.A. 102, 14278-14283
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 14278-14283
    • Kim, S.1    Jeon, T.J.2    Oberai, A.3    Yang, D.4    Schmidt, J.J.5    Bowie, J.U.6
  • 39
    • 44349092071 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis of TM5 reveals conformational changes in OxlT, the oxalate transporter of Oxalobacter formigenes
    • Wang, X., Ye, L., McKinney, C. C., Feng, M. and Maloney, P. C. (2008) Cysteine scanning mutagenesis of TM5 reveals conformational changes in OxlT, the oxalate transporter of Oxalobacter formigenes. Biochemistry 47, 5709-5717
    • (2008) Biochemistry , vol.47 , pp. 5709-5717
    • Wang, X.1    Ye, L.2    McKinney, C.C.3    Feng, M.4    Maloney, P.C.5
  • 40
    • 76749163994 scopus 로고    scopus 로고
    • Simulation of spontaneous substrate binding revealing the binding pathway and mechanism and initial conformational response of GlpT
    • Enkavi, G. and Tajkhorshid, E. (2010) Simulation of spontaneous substrate binding revealing the binding pathway and mechanism and initial conformational response of GlpT. Biochemistry 49, 1105-1114
    • (2010) Biochemistry , vol.49 , pp. 1105-1114
    • Enkavi, G.1    Tajkhorshid, E.2
  • 41
    • 33748651219 scopus 로고    scopus 로고
    • Analysis of substrate-binding elements in OxlT, the oxalate:formate antiporter of Oxalobacter formigenes
    • Wang, X., Sarker, R. I. and Maloney, P. C. (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
  • 43
    • 0000847775 scopus 로고
    • Ionic radii from scaled particle theory of the salt effect
    • Masterton, W. L., Bolocofsky, D. and Lee, T. P. (1971) Ionic radii from scaled particle theory of the salt effect. J. Phys. Chem. 75, 2809-2815
    • (1971) J. Phys. Chem. , vol.75 , pp. 2809-2815
    • Masterton, W.L.1    Bolocofsky, D.2    Lee, T.P.3
  • 44
    • 10044247238 scopus 로고    scopus 로고
    • Structural modeling of dual-affinity purified Pho84 phosphate transporter
    • Lagerstedt, J. O., Voss, J. C., Wieslander, A. and Persson, B. L. (2004) Structural modeling of dual-affinity purified Pho84 phosphate transporter. FEBS Lett. 578, 262-268
    • (2004) FEBS Lett. , vol.578 , pp. 262-268
    • Lagerstedt, J.O.1    Voss, J.C.2    Wieslander, A.3    Persson, B.L.4
  • 45
    • 27744508052 scopus 로고    scopus 로고
    • 3D model of the Escherichia coli multidrug transporter MdfA reveals an essential membrane-embedded positive charge
    • Sigal, N., Vardy, E., Molshanski-Mor, S., Eitan, A., Pilpel, Y., Schuldiner, S. and Bibi, E. (2005) 3D model of the Escherichia coli multidrug transporter MdfA reveals an essential membrane-embedded positive charge. Biochemistry 44, 14870-14880
    • (2005) Biochemistry , vol.44 , pp. 14870-14880
    • Sigal, N.1    Vardy, E.2    Molshanski-Mor, S.3    Eitan, A.4    Pilpel, Y.5    Schuldiner, S.6    Bibi, E.7
  • 46
    • 33846010171 scopus 로고    scopus 로고
    • A three-dimensional model of human organic anion transporter 1: Aromatic amino acids required for substrate transport
    • Perry, J. L, Dembla-Rajpal, N., Hall, L. A. and Pritchard, J. B. (2006) A three-dimensional model of human organic anion transporter 1: aromatic amino acids required for substrate transport. J. Biol. Chem. 281, 38071-38079
    • (2006) J. Biol. Chem. , vol.281 , pp. 38071-38079
    • Perry, J.L.1    Dembla-Rajpal, N.2    Hall, L.A.3    Pritchard, J.B.4
  • 47
    • 79960835280 scopus 로고    scopus 로고
    • A substrate translocation trajectory in a cytoplasm-facing topological model of the monocarboxylate/H+ symporter Jen1p
    • Soares-Silva, I., Sá-Pessoa, J., Myrianthopoulos, V., Mikros, E., Casal, M. and Diallinas, G. (2011) A substrate translocation trajectory in a cytoplasm-facing topological model of the monocarboxylate/H+ symporter Jen1p. Mol. Microbiol. 81, 805-817
    • (2011) Mol. Microbiol. , vol.81 , pp. 805-817
    • Soares-Silva, I.1    Sá-Pessoa, J.2    Myrianthopoulos, V.3    Mikros, E.4    Casal, M.5    Diallinas, G.6
  • 48
    • 77953481979 scopus 로고    scopus 로고
    • Structure-function studies of the SLC17 transporter sialin identify crucial residues and substrate-induced conformational changes
    • Courville, P., Quick, M. and Reimer, R. J. (2010) Structure-function studies of the SLC17 transporter sialin identify crucial residues and substrate-induced conformational changes. J. Biol. Chem. 285, 19316-19323
    • (2010) J. Biol. Chem. , vol.285 , pp. 19316-19323
    • Courville, P.1    Quick, M.2    Reimer, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.