메뉴 건너뛰기




Volumn 348, Issue 3, 2006, Pages 1011-1017

The Na+/H+ antiporter of the thermohalophilic bacterium Rhodothermus marinus

Author keywords

Complex I; Na+ H+ antiporter; Rhodothermus marinus

Indexed keywords

BACTERIAL PROTEIN; LITHIUM ION; MEMBRANE PROTEIN; PROTEIN DERIVATIVE; PROTEIN NHAA; PROTEIN NHAB; PROTEIN NHAC; PROTEIN NHAD; SODIUM ION; SODIUM PROTON EXCHANGE PROTEIN; UNCLASSIFIED DRUG;

EID: 33747176621     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.07.134     Document Type: Article
Times cited : (7)

References (25)
  • 2
    • 26444578862 scopus 로고    scopus 로고
    • The Mrp system: a giant among monovalent cation/proton antiporters?
    • Swartz T.H., Ikewada S., Ishikawa O., Ito M., and Krulwich T.A. The Mrp system: a giant among monovalent cation/proton antiporters?. Extremophiles 9 (2005) 345-354
    • (2005) Extremophiles , vol.9 , pp. 345-354
    • Swartz, T.H.1    Ikewada, S.2    Ishikawa, O.3    Ito, M.4    Krulwich, T.A.5
  • 3
    • 0027536509 scopus 로고
    • Proton-sodium stoichiometry of NhaA, an electrogenic antiporter from Escherichia coli
    • Taglicht D., Padan E., and Schuldiner S. Proton-sodium stoichiometry of NhaA, an electrogenic antiporter from Escherichia coli. J. Biol. Chem. 268 (1993) 5382-5387
    • (1993) J. Biol. Chem. , vol.268 , pp. 5382-5387
    • Taglicht, D.1    Padan, E.2    Schuldiner, S.3
  • 10
    • 1042278126 scopus 로고    scopus 로고
    • Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans
    • Stroh A., Anderka O., Pfeiffer K., Yagi T., Finel M., Ludwig B., and Schagger H. Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans. J. Biol. Chem. 279 (2004) 5000-5007
    • (2004) J. Biol. Chem. , vol.279 , pp. 5000-5007
    • Stroh, A.1    Anderka, O.2    Pfeiffer, K.3    Yagi, T.4    Finel, M.5    Ludwig, B.6    Schagger, H.7
  • 11
    • 0033813865 scopus 로고    scopus 로고
    • Effects of nonpolar mutations in each of the seven Bacillus subtilis mrp genes suggest complex interactions among the gene products in support of Na(+) and alkali but not cholate resistance
    • Ito M., Guffanti A.A., Wang W., and Krulwich T.A. Effects of nonpolar mutations in each of the seven Bacillus subtilis mrp genes suggest complex interactions among the gene products in support of Na(+) and alkali but not cholate resistance. J. Bacteriol. 182 (2000) 5663-5670
    • (2000) J. Bacteriol. , vol.182 , pp. 5663-5670
    • Ito, M.1    Guffanti, A.A.2    Wang, W.3    Krulwich, T.A.4
  • 12
    • 0041563699 scopus 로고    scopus 로고
    • The 'antiporter module' of respiratory chain complex I includes the MrpC/NuoK subunit-a revision of the modular evolution scheme
    • Mathiesen C., and Hagerhall C. The 'antiporter module' of respiratory chain complex I includes the MrpC/NuoK subunit-a revision of the modular evolution scheme. FEBS Lett. 549 (2003) 7-13
    • (2003) FEBS Lett. , vol.549 , pp. 7-13
    • Mathiesen, C.1    Hagerhall, C.2
  • 13
    • 23844456612 scopus 로고    scopus 로고
    • Ion translocation by the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
    • Friedrich T., Stolpe S., Schneider D., Barquera B., and Hellwig P. Ion translocation by the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Biochem. Soc. Trans. 33 (2005) 836-839
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 836-839
    • Friedrich, T.1    Stolpe, S.2    Schneider, D.3    Barquera, B.4    Hellwig, P.5
  • 14
    • 2442473296 scopus 로고    scopus 로고
    • The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton pump but may be capable of secondary sodium antiport
    • Stolpe S., and Friedrich T. The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton pump but may be capable of secondary sodium antiport. J. Biol. Chem. 279 (2004) 18377-18383
    • (2004) J. Biol. Chem. , vol.279 , pp. 18377-18383
    • Stolpe, S.1    Friedrich, T.2
  • 17
    • 0035171171 scopus 로고    scopus 로고
    • Gene cluster of Rhodothermus marinus high-potential iron-sulfur protein: oxygen oxidoreductase, a caa(3)-type oxidase belonging to the superfamily of heme-copper oxidases
    • Santana M., Pereira M.M., Elias N.P., Soares C.M., and Teixeira M. Gene cluster of Rhodothermus marinus high-potential iron-sulfur protein: oxygen oxidoreductase, a caa(3)-type oxidase belonging to the superfamily of heme-copper oxidases. J. Bacteriol. 183 (2001) 687-699
    • (2001) J. Bacteriol. , vol.183 , pp. 687-699
    • Santana, M.1    Pereira, M.M.2    Elias, N.P.3    Soares, C.M.4    Teixeira, M.5
  • 19
    • 3242876311 scopus 로고    scopus 로고
    • BLAST: at the core of a powerful and diverse set of sequence analysis tools
    • McGinnis S., and Madden T.L. BLAST: at the core of a powerful and diverse set of sequence analysis tools. Nucleic Acids Res. 32 (2004) W20-W25
    • (2004) Nucleic Acids Res. , vol.32
    • McGinnis, S.1    Madden, T.L.2
  • 21
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 25
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • Sazanov L.A., and Hinchliffe P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science (2006)
    • (2006) Science
    • Sazanov, L.A.1    Hinchliffe, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.