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Volumn 1818, Issue 5, 2012, Pages 1342-1350

The nitrite transport protein NirC from Salmonella typhimurium is a nitrite/proton antiporter

Author keywords

Acridine orange; Dequenching assay; Nitrite transport; Solid supported membrane; Transport mechanism

Indexed keywords

ANTIPORTER; CARRIER PROTEIN; NITRITE TRANSPORT PROTEIN NIRC; PROTEOLIPOSOME; PROTON; UNCLASSIFIED DRUG;

EID: 84857926522     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2012.02.004     Document Type: Article
Times cited : (29)

References (47)
  • 1
    • 0036024581 scopus 로고    scopus 로고
    • Enzymology and bioenergetics of respiratory nitrite ammonification
    • J. Simon Enzymology and bioenergetics of respiratory nitrite ammonification FEMS Microbiol. Rev. 26 2002 285 309
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 285-309
    • Simon, J.1
  • 2
    • 0033571051 scopus 로고    scopus 로고
    • Competition between Escherichia coli strains expressing either a periplasmic or a membrane-bound nitrate reductase: Does Nap confer a selective advantage during nitrate-limited growth?
    • L.C. Potter, P. Millington, L. Griffiths, G.H. Thomas, and J.A. Cole Competition between Escherichia coli strains expressing either a periplasmic or a membrane-bound nitrate reductase: does Nap confer a selective advantage during nitrate-limited growth? Biochem. J. 344 Pt 1 1999 77 84
    • (1999) Biochem. J. , vol.344 , Issue.PART 1 , pp. 77-84
    • Potter, L.C.1    Millington, P.2    Griffiths, L.3    Thomas, G.H.4    Cole, J.A.5
  • 3
    • 0030019826 scopus 로고    scopus 로고
    • Nitrate reduction to ammonia by enteric bacteria: Redundancy, or a strategy for survival during oxygen starvation?
    • J. Cole Nitrate reduction to ammonia by enteric bacteria: redundancy, or a strategy for survival during oxygen starvation? FEMS Microbiol. Lett. 136 1996 1 11
    • (1996) FEMS Microbiol. Lett. , vol.136 , pp. 1-11
    • Cole, J.1
  • 4
    • 0019799521 scopus 로고
    • The isolation of a hexaheme cytochrome from Desulfovibrio desulfuricans and its identification as a new type of nitrite reductase
    • M.C. Liu, and H.D. Peck Jr. The isolation of a hexaheme cytochrome from Desulfovibrio desulfuricans and its identification as a new type of nitrite reductase J. Biol. Chem. 256 1981 13159 13164
    • (1981) J. Biol. Chem. , vol.256 , pp. 13159-13164
    • Liu, M.C.1    Peck, Jr.H.D.2
  • 5
    • 0025341607 scopus 로고
    • Nucleotide sequence, organisation and structural analysis of the products of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome
    • T. Peakman, J. Crouzet, J.F. Mayaux, S. Busby, S. Mohan, N. Harborne, J. Wootton, R. Nicolson, and J. Cole Nucleotide sequence, organisation and structural analysis of the products of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome Eur. J. Biochem. 191 1990 315 323
    • (1990) Eur. J. Biochem. , vol.191 , pp. 315-323
    • Peakman, T.1    Crouzet, J.2    Mayaux, J.F.3    Busby, S.4    Mohan, S.5    Harborne, N.6    Wootton, J.7    Nicolson, R.8    Cole, J.9
  • 6
    • 0026699489 scopus 로고
    • Transcriptional control, translation and function of the products of the five open reading frames of the Escherichia coli nir operon
    • N.R. Harborne, L. Griffiths, S.J. Busby, and J.A. Cole Transcriptional control, translation and function of the products of the five open reading frames of the Escherichia coli nir operon Mol. Microbiol. 6 1992 2805 2813
    • (1992) Mol. Microbiol. , vol.6 , pp. 2805-2813
    • Harborne, N.R.1    Griffiths, L.2    Busby, S.J.3    Cole, J.A.4
  • 8
    • 0036225848 scopus 로고    scopus 로고
    • The roles of the polytopic membrane proteins NarK, NarU and NirC in Escherichia coli K-12: Two nitrate and three nitrite transporters
    • S. Clegg, F. Yu, L. Griffiths, and J.A. Cole The roles of the polytopic membrane proteins NarK, NarU and NirC in Escherichia coli K-12: two nitrate and three nitrite transporters Mol. Microbiol. 44 2002 143 155
    • (2002) Mol. Microbiol. , vol.44 , pp. 143-155
    • Clegg, S.1    Yu, F.2    Griffiths, L.3    Cole, J.A.4
  • 9
    • 0035105613 scopus 로고    scopus 로고
    • Nitrate and nitrite transport in bacteria
    • J.W. Moir, and N.J. Wood Nitrate and nitrite transport in bacteria Cell. Mol. Life Sci. 58 2001 215 224
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 215-224
    • Moir, J.W.1    Wood, N.J.2
  • 10
    • 0036225747 scopus 로고    scopus 로고
    • Two domains of a dual-function NarK protein are required for nitrate uptake, the first step of denitrification in Paracoccus pantotrophus
    • N.J. Wood, T. Alizadeh, D.J. Richardson, S.J. Ferguson, and J.W. Moir Two domains of a dual-function NarK protein are required for nitrate uptake, the first step of denitrification in Paracoccus pantotrophus Mol. Microbiol. 44 2002 157 170
    • (2002) Mol. Microbiol. , vol.44 , pp. 157-170
    • Wood, N.J.1    Alizadeh, T.2    Richardson, D.J.3    Ferguson, S.J.4    Moir, J.W.5
  • 11
    • 53849131672 scopus 로고    scopus 로고
    • Interdependence of two NarK domains in a fused nitrate/nitrite transporter
    • A.D. Goddard, J.W. Moir, D.J. Richardson, and S.J. Ferguson Interdependence of two NarK domains in a fused nitrate/nitrite transporter Mol. Microbiol. 70 2008 667 681
    • (2008) Mol. Microbiol. , vol.70 , pp. 667-681
    • Goddard, A.D.1    Moir, J.W.2    Richardson, D.J.3    Ferguson, S.J.4
  • 12
    • 33746033796 scopus 로고    scopus 로고
    • Role of the Escherichia coli nitrate transport protein, NarU, in survival during severe nutrient starvation and slow growth
    • S.J. Clegg, W. Jia, and J.A. Cole Role of the Escherichia coli nitrate transport protein, NarU, in survival during severe nutrient starvation and slow growth Microbiology 152 2006 2091 2100
    • (2006) Microbiology , vol.152 , pp. 2091-2100
    • Clegg, S.J.1    Jia, W.2    Cole, J.A.3
  • 13
    • 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
    • W. Jia, N. Tovell, S. Clegg, M. Trimmer, and J. Cole 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 2009 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
  • 14
    • 69949160372 scopus 로고    scopus 로고
    • Novel role of the nitrite transporter NirC in Salmonella pathogenesis: SPI2-dependent suppression of inducible nitric oxide synthase in activated macrophages
    • P. Das, A. Lahiri, A. Lahiri, and D. Chakravortty Novel role of the nitrite transporter NirC in Salmonella pathogenesis: SPI2-dependent suppression of inducible nitric oxide synthase in activated macrophages Microbiology 155 2009 2476 2489
    • (2009) Microbiology , vol.155 , pp. 2476-2489
    • Das, P.1    Lahiri, A.2    Lahiri, A.3    Chakravortty, D.4
  • 15
    • 70849106457 scopus 로고    scopus 로고
    • Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel
    • Y. Wang, Y. Huang, J. Wang, C. Cheng, W. Huang, P. Lu, Y.N. Xu, P. Wang, N. Yan, and Y. Shi Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel Nature 462 2009 467 472
    • (2009) Nature , vol.462 , pp. 467-472
    • Wang, Y.1    Huang, Y.2    Wang, J.3    Cheng, C.4    Huang, W.5    Lu, P.6    Xu, Y.N.7    Wang, P.8    Yan, N.9    Shi, Y.10
  • 16
    • 77449091710 scopus 로고    scopus 로고
    • Structure and mechanism of a pentameric formate channel
    • A.B. Waight, J. Love, and D.N. Wang Structure and mechanism of a pentameric formate channel Nat. Struct. Mol. Biol. 17 2010 31 37
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 31-37
    • Waight, A.B.1    Love, J.2    Wang, D.N.3
  • 17
    • 0037126294 scopus 로고    scopus 로고
    • A biological role for prokaryotic ClC chloride channels
    • R. Iyer, T.M. Iverson, A. Accardi, and C. Miller A biological role for prokaryotic ClC chloride channels Nature 419 2002 715 718
    • (2002) Nature , vol.419 , pp. 715-718
    • Iyer, R.1    Iverson, T.M.2    Accardi, A.3    Miller, C.4
  • 18
    • 33748129976 scopus 로고    scopus 로고
    • Comparative analysis and "expression space" coverage of the production of prokaryotic membrane proteins for structural genomics
    • S. Surade, M. Klein, P.C. Stolt-Bergner, C. Muenke, A. Roy, and H. Michel Comparative analysis and "expression space" coverage of the production of prokaryotic membrane proteins for structural genomics Protein Sci. 15 2006 2178 2189
    • (2006) Protein Sci. , vol.15 , pp. 2178-2189
    • Surade, S.1    Klein, M.2    Stolt-Bergner, P.C.3    Muenke, C.4    Roy, A.5    Michel, H.6
  • 19
    • 24344479129 scopus 로고    scopus 로고
    • Kinetics of charge translocation in the passive downhill uptake mode of the Na+/H + antiporter NhaA of Escherichia coli
    • D. Zuber, R. Krause, M. Venturi, E. Padan, E. Bamberg, and K. Fendler Kinetics of charge translocation in the passive downhill uptake mode of the Na+/H + antiporter NhaA of Escherichia coli Biochim. Biophys. Acta 1709 2005 240 250
    • (2005) Biochim. Biophys. Acta , vol.1709 , pp. 240-250
    • Zuber, D.1    Krause, R.2    Venturi, M.3    Padan, E.4    Bamberg, E.5    Fendler, K.6
  • 21
    • 0022558547 scopus 로고
    • Ion extrusion systems in Escherichia coli
    • B.P. Rosen Ion extrusion systems in Escherichia coli Methods Enzymol. 125 1986 328 336
    • (1986) Methods Enzymol. , vol.125 , pp. 328-336
    • Rosen, B.P.1
  • 22
    • 0018178065 scopus 로고
    • Sodium-proton antiport in isolated membrane vesicles of Escherichia coli
    • S. Schuldiner, and H. Fishkes Sodium-proton antiport in isolated membrane vesicles of Escherichia coli Biochemistry 17 1978 706 711
    • (1978) Biochemistry , vol.17 , pp. 706-711
    • Schuldiner, S.1    Fishkes, H.2
  • 24
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction
    • Y. Cheng, and W.H. Prusoff Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction Biochem. Pharmacol. 22 1973 3099 3108
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 25
    • 39849092319 scopus 로고    scopus 로고
    • One-dimensional SDS gel electrophoresis of proteins
    • 10.2.1-10.2A.37
    • S.R. Gallagher One-dimensional SDS gel electrophoresis of proteins Curr. Protoc. Mol. Biol. 75 2006 10.2.1-10.2A.37
    • (2006) Curr. Protoc. Mol. Biol. , vol.75
    • Gallagher, S.R.1
  • 27
    • 35148876591 scopus 로고    scopus 로고
    • Specific anion and cation binding to lipid membranes investigated on a solid supported membrane
    • J.J. Garcia-Celma, L. Hatahet, W. Kunz, and K. Fendler Specific anion and cation binding to lipid membranes investigated on a solid supported membrane Langmuir 23 2007 10074 10080
    • (2007) Langmuir , vol.23 , pp. 10074-10080
    • Garcia-Celma, J.J.1    Hatahet, L.2    Kunz, W.3    Fendler, K.4
  • 28
    • 0035856526 scopus 로고    scopus 로고
    • Evidence for intraprotein charge transfer during the transport activity of the melibiose permease from Escherichia coli
    • C. Ganea, T. Pourcher, G. Leblanc, and K. Fendler Evidence for intraprotein charge transfer during the transport activity of the melibiose permease from Escherichia coli Biochemistry 40 2001 13744 13752
    • (2001) Biochemistry , vol.40 , pp. 13744-13752
    • Ganea, C.1    Pourcher, T.2    Leblanc, G.3    Fendler, K.4
  • 29
    • 79959553432 scopus 로고    scopus 로고
    • + antiporter NhaA from Escherichia coli: An electrophysiological study
    • + antiporter NhaA from Escherichia coli: an electrophysiological study J. Biol. Chem. 286 2011 23570 23581
    • (2011) J. Biol. Chem. , vol.286 , pp. 23570-23581
    • Mager, T.1    Rimon, A.2    Padan, E.3    Fendler, K.4
  • 30
    • 0015962987 scopus 로고
    • Orientation of membrane vesicles from Escherichia coli as detected by freeze-cleave electron microscopy
    • K.H. Altendorf, and L.A. Staehelin Orientation of membrane vesicles from Escherichia coli as detected by freeze-cleave electron microscopy J. Bacteriol. 117 1974 888 899
    • (1974) J. Bacteriol. , vol.117 , pp. 888-899
    • Altendorf, K.H.1    Staehelin, L.A.2
  • 31
    • 0015993851 scopus 로고
    • Orientation of membrane vesicles from Escherichia coli prepared by different procedures
    • M. Futai Orientation of membrane vesicles from Escherichia coli prepared by different procedures J. Membr. Biol. 15 1974 15 28
    • (1974) J. Membr. Biol. , vol.15 , pp. 15-28
    • Futai, M.1
  • 32
    • 0016703348 scopus 로고
    • Characterization of an active transport system for calcium in inverted membrane vesicles of Escherichia coli
    • T. Tsuchiya, and B.P. Rosen Characterization of an active transport system for calcium in inverted membrane vesicles of Escherichia coli J. Biol. Chem. 250 1975 7687 7692
    • (1975) J. Biol. Chem. , vol.250 , pp. 7687-7692
    • Tsuchiya, T.1    Rosen, B.P.2
  • 33
    • 0018841199 scopus 로고
    • Electrochemical proton gradient in inverted membrane vesicles from Escherichia coli
    • W.W. Reenstra, L. Patel, H. Rottenberg, and H.R. Kaback Electrochemical proton gradient in inverted membrane vesicles from Escherichia coli Biochemistry 19 1980 1 9
    • (1980) Biochemistry , vol.19 , pp. 1-9
    • Reenstra, W.W.1    Patel, L.2    Rottenberg, H.3    Kaback, H.R.4
  • 34
    • 79551496683 scopus 로고    scopus 로고
    • Nitrosative stress in Escherichia coli: Reduction of nitric oxide
    • C.E. Vine, and J.A. Cole Nitrosative stress in Escherichia coli: reduction of nitric oxide Biochem. Soc. Trans. 39 2011 213 215
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 213-215
    • Vine, C.E.1    Cole, J.A.2
  • 35
    • 0031462880 scopus 로고    scopus 로고
    • Direct measurement of nitrite transport across erythrocyte membrane vesicles using the fluorescent probe, 6-methoxy-N-(3-sulfopropyl) quinolinium
    • R. Shingles, M.H. Roh, and R.E. McCarty Direct measurement of nitrite transport across erythrocyte membrane vesicles using the fluorescent probe, 6-methoxy-N-(3-sulfopropyl) quinolinium J. Bioenerg. Biomembr. 29 1997 611 616
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 611-616
    • Shingles, R.1    Roh, M.H.2    McCarty, R.E.3
  • 36
    • 33748310543 scopus 로고    scopus 로고
    • Uncoupling of a CLC Cl-/H + exchange transporter by polyatomic anions
    • W. Nguitragool, and C. Miller Uncoupling of a CLC Cl-/H + exchange transporter by polyatomic anions J. Mol. Biol. 362 2006 682 690
    • (2006) J. Mol. Biol. , vol.362 , pp. 682-690
    • Nguitragool, W.1    Miller, C.2
  • 38
    • 0032692857 scopus 로고    scopus 로고
    • High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel
    • M. Maduke, D.J. Pheasant, and C. Miller High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel J. Gen. Physiol. 114 1999 713 722
    • (1999) J. Gen. Physiol. , vol.114 , pp. 713-722
    • Maduke, M.1    Pheasant, D.J.2    Miller, C.3
  • 40
    • 0031750188 scopus 로고    scopus 로고
    • Permeation and block of the skeletal muscle chloride channel, ClC-1, by foreign anions
    • G.Y. Rychkov, M. Pusch, M.L. Roberts, T.J. Jentsch, and A.H. Bretag Permeation and block of the skeletal muscle chloride channel, ClC-1, by foreign anions J. Gen. Physiol. 111 1998 653 665
    • (1998) J. Gen. Physiol. , vol.111 , pp. 653-665
    • Rychkov, G.Y.1    Pusch, M.2    Roberts, M.L.3    Jentsch, T.J.4    Bretag, A.H.5
  • 42
    • 39149145853 scopus 로고    scopus 로고
    • Nitrite transport is mediated by the nitrite-specific high-affinity NitA transporter and by nitrate transporters NrtA, NrtB in Aspergillus nidulans
    • Y. Wang, W. Li, Y. Siddiqi, V.F. Symington, J.R. Kinghorn, S.E. Unkles, and A.D. Glass Nitrite transport is mediated by the nitrite-specific high-affinity NitA transporter and by nitrate transporters NrtA, NrtB in Aspergillus nidulans Fungal Genet. Biol. 45 2008 94 102
    • (2008) Fungal Genet. Biol. , vol.45 , pp. 94-102
    • Wang, Y.1    Li, W.2    Siddiqi, Y.3    Symington, V.F.4    Kinghorn, J.R.5    Unkles, S.E.6    Glass, A.D.7
  • 43
    • 0033829519 scopus 로고    scopus 로고
    • The Chlamydomonas reinhardtii Nar1 gene encodes a chloroplast membrane protein involved in nitrite transport
    • J. Rexach, E. Fernandez, and A. Galvan The Chlamydomonas reinhardtii Nar1 gene encodes a chloroplast membrane protein involved in nitrite transport Plant Cell 12 2000 1441 1453
    • (2000) Plant Cell , vol.12 , pp. 1441-1453
    • Rexach, J.1    Fernandez, E.2    Galvan, A.3
  • 44
    • 42249089715 scopus 로고    scopus 로고
    • Nitrate assimilation in Chlamydomonas
    • E. Fernandez, and A. Galvan Nitrate assimilation in Chlamydomonas Eukaryot. Cell 7 2008 555 559
    • (2008) Eukaryot. Cell , vol.7 , pp. 555-559
    • Fernandez, E.1    Galvan, A.2
  • 45
    • 33749425963 scopus 로고    scopus 로고
    • Differential regulation of the Chlamydomonas Nar1 gene family by carbon and nitrogen
    • V. Mariscal, P. Moulin, M. Orsel, A.J. Miller, E. Fernandez, and A. Galvan Differential regulation of the Chlamydomonas Nar1 gene family by carbon and nitrogen Protist 157 2006 421 433
    • (2006) Protist , vol.157 , pp. 421-433
    • Mariscal, V.1    Moulin, P.2    Orsel, M.3    Miller, A.J.4    Fernandez, E.5    Galvan, A.6
  • 47
    • 14644387541 scopus 로고    scopus 로고
    • Nitric oxide and nitrosative stress tolerance in bacteria
    • R.K. Poole Nitric oxide and nitrosative stress tolerance in bacteria Biochem. Soc. Trans. 33 2005 176 180
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 176-180
    • Poole, R.K.1


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