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Volumn 585, Issue 8, 2011, Pages 1180-1184

The transmembrane helices of the L, M, and N subunits of Complex i from E. coli can be assigned on the basis of conservation and hydrophobic moment analysis

Author keywords

Complex I; Conservation; Discontinuous helix; Hydrophobic moment; Hydrophobicity; Transmembrane helix

Indexed keywords

REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

EID: 79954435633     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.03.029     Document Type: Article
Times cited : (7)

References (31)
  • 1
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH:quinone oxidoreductase (complex I)
    • DOI 10.1146/annurev.biochem.75.103004.142539
    • U. Brandt Energy converting NADH:quinone oxidoreductase (Complex I) Annu. Rev. Biochem. 75 2006 69 92 (Pubitemid 44118026)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 69-92
    • Brandt, U.1
  • 2
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • DOI 10.1126/science.1123809
    • L.A. Sazanov, and P. Hinchliffe Structure of the hydrophilic domain of respiratory Complex I from Thermus thermophilus Science 311 2006 1430 1436 (Pubitemid 43376691)
    • (2006) Science , vol.311 , Issue.5766 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 3
    • 77952979824 scopus 로고    scopus 로고
    • The architecture of respiratory Complex i
    • R.G. Efremov, R. Baradaran, and L.A. Sazanov The architecture of respiratory Complex I Nature 465 2010 441 445
    • (2010) Nature , vol.465 , pp. 441-445
    • Efremov, R.G.1    Baradaran, R.2    Sazanov, L.A.3
  • 4
    • 77954848120 scopus 로고    scopus 로고
    • Functional modules and structural basis of conformational coupling in mitochondrial Complex i
    • C. Hunte, V. Zickermann, and U. Brandt Functional modules and structural basis of conformational coupling in mitochondrial Complex I Science 329 2010 448 451
    • (2010) Science , vol.329 , pp. 448-451
    • Hunte, C.1    Zickermann, V.2    Brandt, U.3
  • 5
    • 0032490117 scopus 로고    scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    • DOI 10.1016/S0005-2728(98)00024-3, PII S0005272898000243
    • T. Friedrich The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli Biochim. Biophys. Acta 1364 1998 134 146 (Pubitemid 28291836)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1364 , Issue.2 , pp. 134-146
    • Friedrich, T.1
  • 6
    • 33847687662 scopus 로고    scopus 로고
    • Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain
    • DOI 10.1021/bi602508x
    • L.A. Sazanov Respiratory Complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain Biochemistry 46 2007 2275 2288 (Pubitemid 46362402)
    • (2007) Biochemistry , vol.46 , Issue.9 , pp. 2275-2288
    • Sazanov, L.A.1
  • 7
    • 26444578862 scopus 로고    scopus 로고
    • The Mrp system: A giant among monovalent cation/proton antiporters?
    • DOI 10.1007/s00792-005-0451-6
    • T. Swartz, S. Ikewada, O. Ishikawa, M. Ito, and T. Krulwich The Mrp system: a giant among monovalent cation/proton antiporters? Extremophiles 9 2005 345 354 (Pubitemid 41428347)
    • (2005) Extremophiles , vol.9 , Issue.5 , pp. 345-354
    • Swartz, T.H.1    Ikewada, S.2    Ishikawa, O.3    Ito, M.4    Krulwich, T.A.5
  • 8
    • 0242322000 scopus 로고    scopus 로고
    • The Location of NuoL and NuoM Subunits in the Membrane Domain of the Escherichia coli Complex I: Implications for the mechanism of proton pumping
    • DOI 10.1074/jbc.M308247200
    • P.J. Holt, D.J. Morgan, and L.A. Sazanov The location of NuoL and NuoM subunits in the membrane domain of the Escherichia coli complex I: implications for the mechanism of proton pumping J. Biol. Chem. 278 2003 43114 43120 (Pubitemid 37345929)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.44 , pp. 43114-43120
    • Holt, P.J.1    Morgan, D.J.2    Sazanov, L.A.3
  • 9
    • 77957107068 scopus 로고    scopus 로고
    • A new hypothesis on the simultaneous direct and indirect proton pump mechanisms in NADH-quinone oxidoreductase (complex I)
    • T. Ohnishi, E. Nakamaru-Ogiso, and S.T. Ohnishi A new hypothesis on the simultaneous direct and indirect proton pump mechanisms in NADH-quinone oxidoreductase (complex I) FEBS Lett. 584 2010 4131 4137
    • (2010) FEBS Lett. , vol.584 , pp. 4131-4137
    • Ohnishi, T.1    Nakamaru-Ogiso, E.2    Ohnishi, S.T.3
  • 11
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • DOI 10.1016/0022-2836(84)90309-7
    • D. Eisenberg, E. Schwarz, M. Komaromy, and R. Wall Analysis of membrane and surface protein sequences with the hydrophobic moment plot J. Mol. Biol. 179 1984 125 142 (Pubitemid 16223392)
    • (1984) Journal of Molecular Biology , vol.179 , Issue.1 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 13
    • 0026479944 scopus 로고
    • o ATP synthase using variational and hydrophobic moment analyses
    • o ATP synthase using variational and hydrophobic moment analyses Biochim. Biophys. Acta 1140 1992 199 207
    • (1992) Biochim. Biophys. Acta , vol.1140 , pp. 199-207
    • Vik, S.B.1    Dao, N.N.2
  • 14
    • 4444382786 scopus 로고    scopus 로고
    • A knowledge-based scale for the analysis and prediction of buried and exposed faces of transmembrane domain proteins
    • DOI 10.1093/bioinformatics/bth143
    • T. Beuming, and H. Weinstein A knowledge-based scale for the analysis and prediction of buried and exposed faces of transmembrane domain proteins Bioinformatics 20 2004 1822 1835 (Pubitemid 39199046)
    • (2004) Bioinformatics , vol.20 , Issue.12 , pp. 1822-1835
    • Beuming, T.1    Weinstein, H.2
  • 15
    • 0034843597 scopus 로고    scopus 로고
    • AL2CO: Calculation of positional conservation in a protein sequence alignment
    • J. Pei, and N.V. Grishin AL2CO: calculation of positional conservation in a protein sequence alignment Bioinformatics 17 2001 700 712 (Pubitemid 32851378)
    • (2001) Bioinformatics , vol.17 , Issue.8 , pp. 700-712
    • Pei, J.1    Grishin, N.V.2
  • 16
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • G. von Heijne Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule J. Mol. Biol. 225 1992 487 494
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 17
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • D.M. Engelman, T.A. Steitz, and A. Goldman Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins Annu. Rev. Biophys. Biophys. Chem. 15 1986 321 353
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 321-353
    • Engelman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 18
    • 0026605537 scopus 로고
    • CLUSTAL V: Improved software for multiple sequence alignment
    • D.G. Higgins, A.J. Bleasby, and R. Fuchs CLUSTAL V: improved software for multiple sequence alignment Comput. Appl. Biosci. 8 1992 189 191
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 189-191
    • Higgins, D.G.1    Bleasby, A.J.2    Fuchs, R.3
  • 19
    • 34447637751 scopus 로고    scopus 로고
    • Discontinuous membrane helices in transport proteins and their correlation with function
    • DOI 10.1016/j.jsb.2007.01.011, PII S1047847707000317
    • E. Screpanti, and C. Hunte Discontinuous membrane helices in transport proteins and their correlation with function J. Struct. Biol. 159 2007 261 267 (Pubitemid 47095395)
    • (2007) Journal of Structural Biology , vol.159 , Issue.SPEC. ISS. 2 , pp. 261-267
    • Screpanti, E.1    Hunte, C.2
  • 21
    • 64649090099 scopus 로고    scopus 로고
    • Characterization of the functionally critical AXAXAXA and PXXEXXP Motifs of the ATP synthase c-Subunit from an Alkaliphilic Bacillus
    • J. Liu, M. Fujisawa, D.B. Hicks, and T.A. Krulwich Characterization of the functionally critical AXAXAXA and PXXEXXP Motifs of the ATP synthase c-Subunit from an Alkaliphilic Bacillus J. Biol. Chem. 284 2009 8714 8725
    • (2009) J. Biol. Chem. , vol.284 , pp. 8714-8725
    • Liu, J.1    Fujisawa, M.2    Hicks, D.B.3    Krulwich, T.A.4
  • 22
    • 0035979710 scopus 로고    scopus 로고
    • Atomic structure of a glycerol channel and implications for substrate permeation in aqua(glycero)porins
    • DOI 10.1016/S0014-5793(01)02710-7, PII S0014579301027107
    • P. Nollert, W.E.C. Harries, D. Fu, L.J.W. Miercke, and R.M. Stroud Atomic structure of a glycerol channel and implications for substrate permeation in aqua(glycero)porins FEBS Lett. 504 2001 112 117 (Pubitemid 32787058)
    • (2001) FEBS Letters , vol.504 , Issue.3 , pp. 112-117
    • Nollert, P.1    Harries, W.E.C.2    Fu, D.3    Miercke, L.J.W.4    Stroud, R.M.5
  • 23
    • 77957128550 scopus 로고    scopus 로고
    • Truncation of subunit ND2 disrupts the threefold symmetry of the antiporter-like subunits in complex i from higher metazoans
    • J.A. Birrell, and J. Hirst Truncation of subunit ND2 disrupts the threefold symmetry of the antiporter-like subunits in complex I from higher metazoans FEBS Lett. 584 2010 4247 4252
    • (2010) FEBS Lett. , vol.584 , pp. 4247-4252
    • Birrell, J.A.1    Hirst, J.2
  • 24
    • 0037010862 scopus 로고    scopus 로고
    • Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters
    • DOI 10.1016/S0005-2728(02)00343-2, PII S0005272802003432
    • C. Mathiesen, and C. Hägerhäll Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters Biochim. Biophys. Acta 1556 2002 121 132 (Pubitemid 35379670)
    • (2002) Biochimica et Biophysica Acta - Bioenergetics , vol.1556 , Issue.2-3 , pp. 121-132
    • Mathiesen, C.1    Hagerhall, C.2
  • 25
    • 70549113296 scopus 로고    scopus 로고
    • Features of subunit NuoM (ND4) in Escherichia coli NDH-1: Topology and implication of conserved Glu144 for coupling site 1
    • J. Torres-Bacete, P.K. Sinha, N. Castro-Guerrero, A. Matsuno-Yagi, and T. Yagi Features of subunit NuoM (ND4) in Escherichia coli NDH-1: Topology and implication of conserved Glu144 for coupling site 1 J. Biol. Chem. 284 2009 33062 33069
    • (2009) J. Biol. Chem. , vol.284 , pp. 33062-33069
    • Torres-Bacete, J.1    Sinha, P.K.2    Castro-Guerrero, N.3    Matsuno-Yagi, A.4    Yagi, T.5
  • 26
    • 78751641992 scopus 로고    scopus 로고
    • Transmembrane topology of subunit N of complex i (NADH:ubiquinone oxidoreductase) from Escherichia coli
    • B. Amarneh, and S.B. Vik Transmembrane topology of subunit N of complex I (NADH:ubiquinone oxidoreductase) from Escherichia coli J. Bioenerg. Biomembr. 42 2010 511 516
    • (2010) J. Bioenerg. Biomembr. , vol.42 , pp. 511-516
    • Amarneh, B.1    Vik, S.B.2
  • 27
    • 0037995650 scopus 로고    scopus 로고
    • Mutagenesis of subunit N of the Escherichia coli Complex I. Identification of the initiation codon and the sensitivity of mutants to decylubiquinone
    • DOI 10.1021/bi0340346
    • B. Amarneh, and S.B. Vik Mutagenesis of subunit N of the Escherichia coli Complex I. Identification of the initiation codon and the sensitivity of mutants to decylubiquinone Biochemistry 42 2003 4800 4808 (Pubitemid 36532031)
    • (2003) Biochemistry , vol.42 , Issue.17 , pp. 4800-4808
    • Amarneh, B.1    Vik, S.B.2
  • 28
    • 37549049790 scopus 로고    scopus 로고
    • Characterization of the nuoM (ND4) subunit in Escherichia coli NDH-1: Conserved charged residues essential for energy-coupled activities
    • J. Torres-Bacete, E. Nakamaru-Ogiso, A. Matsuno-Yagi, and T. Yagi Characterization of the nuoM (ND4) subunit in Escherichia coli NDH-1: conserved charged residues essential for energy-coupled activities J. Biol. Chem. 282 2007 36914 36922
    • (2007) J. Biol. Chem. , vol.282 , pp. 36914-36922
    • Torres-Bacete, J.1    Nakamaru-Ogiso, E.2    Matsuno-Yagi, A.3    Yagi, T.4
  • 29
    • 49349107465 scopus 로고    scopus 로고
    • Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase (Complex I)
    • L. Euro, G. Belevich, M.I. Verkhovsky, M. Wikström, and M. Verkhovskaya Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase (Complex I) Biochim. Biophys. Acta 1777 2008 1166 1172
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1166-1172
    • Euro, L.1    Belevich, G.2    Verkhovsky, M.I.3    Wikström, M.4    Verkhovskaya, M.5
  • 30
    • 78649496491 scopus 로고    scopus 로고
    • The membrane subunit NuoL(ND5) is involved in the indirect proton pumping mechanism of E. coli complex i
    • E. Nakamaru-Ogiso, M.C. Kao, H. Chen, S.C. Sinha, T. Yagi, and T. Ohnishi The membrane subunit NuoL(ND5) is involved in the indirect proton pumping mechanism of E. coli complex I J. Biol. Chem. 285 2010 39070 39078
    • (2010) J. Biol. Chem. , vol.285 , pp. 39070-39078
    • Nakamaru-Ogiso, E.1    Kao, M.C.2    Chen, H.3    Sinha, S.C.4    Yagi, T.5    Ohnishi, T.6
  • 31
    • 79952236392 scopus 로고    scopus 로고
    • Mutagenesis of the L, M, and N subunits of Complex i from Escherichia coli indicates a common role in function
    • J. Michel, J. DeLeon-Rangel, S. Zhu, K. Van Ree, and S.B. Vik Mutagenesis of the L, M, and N subunits of Complex I from Escherichia coli indicates a common role in function PLoS ONE 6 2011 e17420
    • (2011) PLoS ONE , vol.6 , pp. 17420
    • Michel, J.1    Deleon-Rangel, J.2    Zhu, S.3    Van Ree, K.4    Vik, S.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.