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Volumn 445, Issue 1, 2014, Pages 80-86

The Na+ transport in gram-positive bacteria defect in the Mrp antiporter complex measured with 23Na nuclear magnetic resonance

Author keywords

Bacillus subtilis; Cation proton antiporter 3 family; Membrane transport; Mrp antiporter; NMR; Sodium concentration

Indexed keywords

BACTERIA; BACTERIOLOGY; GENE ENCODING; LIPOSOMES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POSITIVE IONS;

EID: 84888116310     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2013.10.003     Document Type: Article
Times cited : (14)

References (36)
  • 2
    • 0032897180 scopus 로고    scopus 로고
    • + antiporter gene which is important for pH homeostasis of alkaliphilic Bacillus sp. C-125
    • DOI 10.1016/S0005-2728(98)00157-1, PII S0005272898001571
    • + antiporter gene which is important for pH homeostasis of alkaliphilic Bacillus sp. C-125 Biochim. Biophys. Acta 1409 1999 171 175 (Pubitemid 29044066)
    • (1999) Biochimica et Biophysica Acta - Bioenergetics , vol.1409 , Issue.3 , pp. 171-175
    • Kosono, S.1    Morotomi, S.2    Kitada, M.3    Kudo, T.4
  • 3
    • 22544452689 scopus 로고    scopus 로고
    • Characterization of a multigene-encoded sodium/hydrogen antiporter (Sha) from Pseudomonas aeruginosa: Its involvement in pathogenesis
    • DOI 10.1128/JB.187.15.5242-5248.2005
    • S. Kosono, K. Haga, R. Tomizawa, Y. Kajiyama, K. Hatano, S. Takeda, Y. Wakai, M. Hino, and T. Kudo Characterization of a multigene-encoded sodium/hydrogen antiporter (sha) from Pseudomonas aeruginosa: its involvement in pathogenesis J. Bacteriol. 187 2005 5242 5248 (Pubitemid 41022943)
    • (2005) Journal of Bacteriology , vol.187 , Issue.15 , pp. 5242-5248
    • Kosono, S.1    Haga, K.2    Tomizawa, R.3    Kajiyama, Y.4    Hatano, K.5    Takeda, S.6    Wakai, Y.7    Hino, M.8    Kudo, T.9
  • 6
    • 44949253200 scopus 로고    scopus 로고
    • + antiporter of alkaliphilic Bacillus and formation of hetero-oligomeric Mrp complexes
    • DOI 10.1128/JB.00294-08
    • + antiporter of alkaliphilic Bacillus and formation of hetero-oligomeric Mrp complexes J. Bacteriol. 190 2008 4162 4172 (Pubitemid 351812862)
    • (2008) Journal of Bacteriology , vol.190 , Issue.12 , pp. 4162-4172
    • Morino, M.1    Natsui, S.2    Swartz, T.H.3    Krulwich, T.A.4    Ito, M.5
  • 10
    • 69949185951 scopus 로고    scopus 로고
    • The MrpA, MrpB, and MrpD subunits of the Mrp antiporter complex in Bacillus subtilis contain membrane-embedded and essential acidic residues
    • Y. Kajiyama, M. Otagiri, J. Sekiguchi, T. Kudo, and S. Kosono The MrpA, MrpB, and MrpD subunits of the Mrp antiporter complex in Bacillus subtilis contain membrane-embedded and essential acidic residues Microbiology 155 2009 2137 2147
    • (2009) Microbiology , vol.155 , pp. 2137-2147
    • Kajiyama, Y.1    Otagiri, M.2    Sekiguchi, J.3    Kudo, T.4    Kosono, S.5
  • 11
    • 0026484793 scopus 로고
    • Conservation of sequences of subunits of mitochondrial complex i and their relationships with other proteins
    • I.M. Fearnley, and J.E. Walker Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins Biochim. Biophys. Acta 1140 1992 105 134
    • (1992) Biochim. Biophys. Acta , vol.1140 , pp. 105-134
    • Fearnley, I.M.1    Walker, J.E.2
  • 12
    • 80052068980 scopus 로고    scopus 로고
    • Structure of the membrane domain of respiratory complex i
    • R.G. Efremov, and L.A. Sazanov Structure of the membrane domain of respiratory complex I Nature 476 2011 414 420
    • (2011) Nature , vol.476 , pp. 414-420
    • Efremov, R.G.1    Sazanov, L.A.2
  • 13
    • 79751524661 scopus 로고    scopus 로고
    • Homologous protein subunits from Escherichia coli NADH: Quinone oxidoreductase can functionally replace MrpA and MrpD in Bacillus subtilis
    • V.K. Moparthi, B. Kumar, C. Mathiesen, and C. Hägerhäll Homologous protein subunits from Escherichia coli NADH:quinone oxidoreductase can functionally replace MrpA and MrpD in Bacillus subtilis Biochim. Biophys. Acta 1807 2011 427 436
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 427-436
    • Moparthi, V.K.1    Kumar, B.2    Mathiesen, C.3    Hägerhäll, C.4
  • 15
    • 84888645927 scopus 로고    scopus 로고
    • The ion-translocation activities of proteins from Mrp-antiporter family, evolutionarily related to complex I, analyzed in a Bacillus subtilis model system
    • E. Sperling, V.K. Moparthi, B. Kumar, Y. Al-Eryani, E. Virzintiene, and C. Hägerhäll The ion-translocation activities of proteins from Mrp-antiporter family, evolutionarily related to complex I, analyzed in a Bacillus subtilis model system Biochim. Biophys. Acta 1817 2012 S61
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 61
    • Sperling, E.1    Moparthi, V.K.2    Kumar, B.3    Al-Eryani, Y.4    Virzintiene, E.5    Hägerhäll, C.6
  • 16
    • 0027750782 scopus 로고
    • + exchange by Escherichia coli NhaA in reconstituted proteoliposomes
    • DOI 10.1016/0014-5793(93)80869-V
    • + exchange by Escherichia coli NhaA in reconstituted proteoliposomes FEBS Lett. 336 1993 525 529 (Pubitemid 24037012)
    • (1993) FEBS Letters , vol.336 , Issue.3 , pp. 525-529
    • Dibrov, P.A.1
  • 17
    • 0038712412 scopus 로고    scopus 로고
    • +
    • DOI 10.1074/jbc.M301682200
    • +-dependent complex I from Escherichia coli transports Na J. Biol. Chem. 278 2003 26817 26822 (Pubitemid 36876831)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.29 , pp. 26817-26822
    • Steuber, J.1
  • 19
    • 0034212749 scopus 로고    scopus 로고
    • +-ATPase by persistent sodium accumulation in adult rat thalamic neurones
    • V.V. Senatorov, P.K. Stys, and B. Hu Regulation of Na+, K+-ATPase by persistent sodium accumulation in adult rat thalamic neurones J. Physiol. 525 2000 343 353 (Pubitemid 30398365)
    • (2000) Journal of Physiology , vol.525 , Issue.2 , pp. 343-353
    • Senatorov, V.V.1    Stys, P.K.2    Hu, B.3
  • 20
    • 33646163009 scopus 로고    scopus 로고
    • Fluorescence measurement of intracellular sodium concentration in single Escherichia coli cells
    • C.-J. Lo, M.C. Leake, and R.M. Berry Fluorescence measurement of intracellular sodium concentration in single Escherichia coli cells Biophys. J. 90 2006 357 365
    • (2006) Biophys. J. , vol.90 , pp. 357-365
    • Lo, C.-J.1    Leake, M.C.2    Berry, R.M.3
  • 22
    • 78650930448 scopus 로고    scopus 로고
    • Sodium influence on energy transduction by complexes i from Escherichia coli and Paracoccus denitrificans
    • A.P. Batista, and M.M. Pereira Sodium influence on energy transduction by complexes I from Escherichia coli and Paracoccus denitrificans Biochim. Biophys. Acta 1807 2011 286 292
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 286-292
    • Batista, A.P.1    Pereira, M.M.2
  • 23
    • 0028986049 scopus 로고
    • + in the halotolerant bacterium Brevibacterium sp. and Escherichia coli
    • + in the halotolerant bacterium Brevibacterium sp. and Escherichia coli Microbiology 140 1995 729 736
    • (1995) Microbiology , vol.140 , pp. 729-736
    • Nagata, S.1    Adachi, K.2    Shirai, K.3    Sano, H.4
  • 24
    • 84861311149 scopus 로고    scopus 로고
    • The role of proton and sodium ions in energy transduction by respiratory complex i
    • A.P. Batista, B.C. Marreiros, and M.M. Pereira The role of proton and sodium ions in energy transduction by respiratory complex I IUBMB Life 64 2012 492 498
    • (2012) IUBMB Life , vol.64 , pp. 492-498
    • Batista, A.P.1    Marreiros, B.C.2    Pereira, M.M.3
  • 25
    • 79957477189 scopus 로고    scopus 로고
    • Decoupling of the catalytic and transport activities of complex i from Rhodothermus marinus by sodium/proton antiporter inhibitor
    • A.P. Batista, B.C. Marreiros, and M.M. Pereira Decoupling of the catalytic and transport activities of complex I from Rhodothermus marinus by sodium/proton antiporter inhibitor ACS Chem. Biol. 6 2011 477 483
    • (2011) ACS Chem. Biol. , vol.6 , pp. 477-483
    • Batista, A.P.1    Marreiros, B.C.2    Pereira, M.M.3
  • 26
    • 77955105850 scopus 로고    scopus 로고
    • A cytochrome c fusion protein domain for convenient detection, quantification, and enhanced production of membrane proteins in Escherichia coli: Expression and characterization of cytochrome-tagged complex i subunits
    • T. Gustavsson, M. Trane, V.K. Moparthi, E. Miklovyte, L. Moparthi, K. Górecki, T. Leiding, S.P. Årsköld, and C. Hägerhäll A cytochrome c fusion protein domain for convenient detection, quantification, and enhanced production of membrane proteins in Escherichia coli: expression and characterization of cytochrome-tagged complex I subunits Protein Sci. 19 2010 1445 1460
    • (2010) Protein Sci. , vol.19 , pp. 1445-1460
    • Gustavsson, T.1    Trane, M.2    Moparthi, V.K.3    Miklovyte, E.4    Moparthi, L.5    Górecki, K.6    Leiding, T.7    Årsköld, S.P.8    Hägerhäll, C.9
  • 27
    • 84888638558 scopus 로고    scopus 로고
    • Gnuplot 4.4: An interactive plotting program
    • Gnuplot 4.4: An interactive plotting program, http://gnuplot.sourceforge. net.
  • 28
    • 0013786935 scopus 로고
    • Nuclear magnetic resonance evidence for complexing of sodium ions in muscle
    • F.W. Cope Nuclear magnetic resonance evidence for complexing of sodium ions in muscle Proc. Natl. Acad. Sci. U.S.A. 54 1965 225 227
    • (1965) Proc. Natl. Acad. Sci. U.S.A. , vol.54 , pp. 225-227
    • Cope, F.W.1
  • 29
    • 0015254103 scopus 로고
    • Nuclear magnetic resonance of sodium-23 linoleate-water: Basis for an alternative interpretation of sodium-23 spectra within cells
    • M. Shporer, and M.M. Civan Nuclear magnetic resonance of sodium-23 linoleate-water: basis for an alternative interpretation of sodium-23 spectra within cells Biophys. J. 12 1972 114 122
    • (1972) Biophys. J. , vol.12 , pp. 114-122
    • Shporer, M.1    Civan, M.M.2
  • 30
    • 0024332209 scopus 로고
    • Ion interactions at membranous polypeptide sites using nuclear magnetic resonance: Determining rate and binding constants and site locations
    • DOI 10.1016/S0076-6879(89)71018-1
    • D.W. Urry, T.L. Trapane, C.M. Venkatachalam, and R.B. McMichens Ion interactions at membranous polypeptide sites using nuclear magnetic resonance: determining rate and binding constants and site locations Methods Enzymol. 171 1989 286 342 (Pubitemid 20010206)
    • (1989) Methods in Enzymology , vol.171 , pp. 286-342
    • Urry, D.W.1    Trapane, T.L.2    Venkatachalam, C.M.3    McMichens, R.B.4
  • 33
    • 0000058888 scopus 로고
    • 23Na-NMR studies of the intracellular sodium ion concentration in the halotolerant alga Dunaliella salina
    • 23Na-NMR studies of the intracellular sodium ion concentration in the halotolerant alga Dunaliella salina Plant Physiol. 87 1988 813 817
    • (1988) Plant Physiol. , vol.87 , pp. 813-817
    • Bental, M.1    Degani, H.2    Avron, M.3
  • 34
    • 0025919703 scopus 로고
    • 23Na nuclear magnetic resonance spectroscopy to determine the true intracellular concentration of free sodium in a halophile eubacterium
    • 23Na nuclear magnetic resonance spectroscopy to determine the true intracellular concentration of free sodium in a halophile eubacterium J. Bacteriol. 173 1991 7021 7023
    • (1991) J. Bacteriol. , vol.173 , pp. 7021-7023
    • Gilboa, H.1    Kogut, M.2    Chalamish, S.3    Regev, R.4    Avi-Dor, Y.5    Russell, N.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.