Genomes and Genes
Gene Symbol: nuoI
Description: NADH:ubiquinone oxidoreductase, chain I
Alias: ECK2275, JW2276
Species: Escherichia coli str. K-12 substr. MG1655
- Sazanov L. Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry. 2007;46:2275-88 pubmed..In this review, novel mechanistic implications of the structure are discussed, and the effects of many known mutations of complex I subunits are interpreted in a structural context. ..
- Archer C, Elliott T. Transcriptional control of the nuo operon which encodes the energy-conserving NADH dehydrogenase of Salmonella typhimurium. J Bacteriol. 1995;177:2335-42 pubmed..Mutations in the global regulatory genes arcA, oxrA (fnr), crp, cya, and katF were tested for effects on expression of the nuo operon. However, none of the mutations tested had a large effect on expression of type I NADH dehydrogenase. ..
- Gemperli A, Schaffitzel C, Jakob C, Steuber J. Transport of Na(+) and K (+) by an antiporter-related subunit from the Escherichia coli NADH dehydrogenase I produced in Saccharomyces cerevisiae. Arch Microbiol. 2007;188:509-21 pubmed..The cation selectivity and function of the NuoL subunit as a transporter module of the NADH dehydrogenase complex is discussed. ..
- Leif H, Sled V, Ohnishi T, Weiss H, Friedrich T. Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli. Eur J Biochem. 1995;230:538-48 pubmed..This subunit arrangement coincidences to some extent with the order of the genes on the nuo operon. A topological model of the E. coli complex I is proposed...
- Ohnishi T, Nakamaru Ogiso E. Were there any "misassignments" among iron-sulfur clusters N4, N5 and N6b in NADH-quinone oxidoreductase (complex I)?. Biochim Biophys Acta. 2008;1777:703-10 pubmed publisher..Therefore, we believe that we have not made any "misassignment" in our work. ..
- Rasmussen T, Scheide D, Brors B, Kintscher L, Weiss H, Friedrich T. Identification of two tetranuclear FeS clusters on the ferredoxin-type subunit of NADH:ubiquinone oxidoreductase (complex I). Biochemistry. 2001;40:6124-31 pubmed..3c of the N. crassa or NuoI of the E. coli complex I, respectively...
- Friedrich T. Complex I: a chimaera of a redox and conformation-driven proton pump?. J Bioenerg Biomembr. 2001;33:169-77 pubmed..This implies that complex I contains two energy-coupling sites. The NADH dehydrogenase module seems to be involved in electron transfer and not in proton translocation. ..
- Sinha P, Nakamaru Ogiso E, Torres Bacete J, Sato M, Castro Guerrero N, Ohnishi T, et al. Electron transfer in subunit NuoI (TYKY) of Escherichia coli NADH:quinone oxidoreductase (NDH-1). J Biol Chem. 2012;287:17363-73 pubmed publisher..Subunit NuoI in the peripheral domain contains two [4Fe-4S] clusters (N6a and N6b) and plays a role in bridging the electron ..
- Bungert S, Krafft B, Schlesinger R, Friedrich T. One-step purification of the NADH dehydrogenase fragment of the Escherichia coli complex I by means of Strep-tag affinity chromatography. FEBS Lett. 1999;460:207-11 pubmed..This was achieved by fusing the Strep-tag II peptide to the C-terminus of NuoF or NuoG. Fusion of this peptide to the N-terminus of either NuoE or NuoF disturbed the assembly of the NADH dehydrogenase fragment. ..
- Gong X, Xie T, Yu L, Hesterberg M, Scheide D, Friedrich T, et al. The ubiquinone-binding site in NADH:ubiquinone oxidoreductase from Escherichia coli. J Biol Chem. 2003;278:25731-7 pubmed..Using the PHDhtm hydropathy plot, the labeled peptide is located in the transmembrane helix 4 toward the periplasmic side of the membrane. ..
- Kao M, Di Bernardo S, Nakamaru Ogiso E, Miyoshi H, Matsuno Yagi A, Yagi T. Characterization of the membrane domain subunit NuoJ (ND6) of the NADH-quinone oxidoreductase from Escherichia coli by chromosomal DNA manipulation. Biochemistry. 2005;44:3562-71 pubmed..Together with the results on mutations related to human diseases, possible functional roles of the NuoJ subunit have been discussed. ..
- Kao M, Nakamaru Ogiso E, Matsuno Yagi A, Yagi T. Characterization of the membrane domain subunit NuoK (ND4L) of the NADH-quinone oxidoreductase from Escherichia coli. Biochemistry. 2005;44:9545-54 pubmed..Possible roles of these arginine residues and other conserved residues in the NuoK subunit for NDH-1 function were discussed. ..
- Amarneh B, De Leon Rangel J, Vik S. Construction of a deletion strain and expression vector for the Escherichia coli NADH:ubiquinone oxidoreductase (Complex I). Biochim Biophys Acta. 2006;1757:1557-60 pubmed..A chromosomal deletion of all nuo genes has been achieved by homologous recombination. A vector that encodes all of the nuo genes has been constructed, and it expresses a functional enzyme. ..
- Baranova E, Holt P, Sazanov L. Projection structure of the membrane domain of Escherichia coli respiratory complex I at 8 A resolution. J Mol Biol. 2007;366:140-54 pubmed
- Schneider D, Pohl T, Walter J, Dörner K, Kohlstädt M, Berger A, et al. Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Biochim Biophys Acta. 2008;1777:735-9 pubmed publisher..It is discussed whether this fragment represents an assembly intermediate. In addition, a membrane-bound fragment exhibiting NADH/ferricyanide oxidoreductase activity and containing the iron-sulfur cluster N2 was detected in one mutant. ..
- Zambrano M, Kolter R. Escherichia coli mutants lacking NADH dehydrogenase I have a competitive disadvantage in stationary phase. J Bacteriol. 1993;175:5642-7 pubmed..This is the first identification of genes encoding subunits of NADH dehydrogenase I in E. coli. The significance of the inability of these mutant strains to compete in stationary-phase cultures is discussed. ..
- Braun M, Bungert S, Friedrich T. Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochemistry. 1998;37:1861-7 pubmed..The preparation fulfills all prerequisites for crystallization of the fragment. ..
- Tran Q, Bongaerts J, Vlad D, Unden G. Requirement for the proton-pumping NADH dehydrogenase I of Escherichia coli in respiration of NADH to fumarate and its bioenergetic implications. Eur J Biochem. 1997;244:155-60 pubmed..NADH-->dimethylsulfoxide respiration is also dependent on NADH dehydrogenase I. The consequences for energy conservation by anaerobic respiration with NADH as a donor are discussed. ..
- Calhoun M, Oden K, Gennis R, de Mattos M, Neijssel O. Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain. J Bacteriol. 1993;175:3020-5 pubmed
- Spehr V, Schlitt A, Scheide D, Guenebaut V, Friedrich T. Overexpression of the Escherichia coli nuo-operon and isolation of the overproduced NADH:ubiquinone oxidoreductase (complex I). Biochemistry. 1999;38:16261-7 pubmed..Due to its stability over a wide pH range and at very high salt concentrations, this preparation is well suited for structural investigations. ..
- Nakamaru Ogiso E, Matsuno Yagi A, Yoshikawa S, Yagi T, Ohnishi T. Iron-sulfur cluster N5 is coordinated by an HXXXCXXCXXXXXC motif in the NuoG subunit of Escherichia coli NADH:quinone oxidoreductase (complex I). J Biol Chem. 2008;283:25979-87 pubmed publisher..These data confirmed that, contrary to the misassignment claim, cluster N5 has a unique coordination with His(Cys)(3) ligands in NuoG. ..
- Morgan D, Sazanov L. Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides. Biochim Biophys Acta. 2008;1777:711-8 pubmed publisher..The model of the entire bacterial complex I could be built from the crystal structures of subcomplexes using the EM envelope described here. ..
- Bongaerts J, Zoske S, Weidner U, Unden G. Transcriptional regulation of the proton translocating NADH dehydrogenase genes (nuoA-N) of Escherichia coli by electron acceptors, electron donors and gene regulators. Mol Microbiol. 1995;16:521-34 pubmed..A physiological role for the transcriptional stimulation by O2 and nitrate is suggested. ..
- Yakovlev G, Reda T, Hirst J. Reevaluating the relationship between EPR spectra and enzyme structure for the iron sulfur clusters in NADH:quinone oxidoreductase. Proc Natl Acad Sci U S A. 2007;104:12720-5 pubmed..Consequently, we propose that EPR signals N4 and N5 have been misassigned: signal N4 is from NuoI (not NuoG) and signal N5 is from the conserved cysteine-ligated [4Fe-4S] cluster in NuoG (not from the cluster with ..
- Weidner U, Geier S, Ptock A, Friedrich T, Leif H, Weiss H. The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I. J Mol Biol. 1993;233:109-22 pubmed publisher..To some extent, the gene order correlates with the topological arrangement of the encoded subunits. The conception of modular evolution of NADH: ubiquinone oxidoreductase is further supported by the arrangement of the nuo-genes...
- Stolpe S, 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. 2004;279:18377-83 pubmed..coli complex I is a primary electrogenic proton pump. However, the magnitude of the pH gradient depended on the sodium concentration. The capability of complex I for secondary Na(+)/H(+) antiport is discussed. ..
- Moreno Bruna B, Baroja Fernandez E, Munoz F, Bastarrica Berasategui A, Zandueta Criado A, Rodriguez Lopez M, et al. Adenosine diphosphate sugar pyrophosphatase prevents glycogen biosynthesis in Escherichia coli. Proc Natl Acad Sci U S A. 2001;98:8128-32 pubmed..The overall results pinpoint the reaction catalyzed by ASPPase as a potential step of regulating glycogen biosynthesis in E. coli. ..
- Ohnishi T. Iron-sulfur clusters/semiquinones in complex I. Biochim Biophys Acta. 1998;1364:186-206 pubmed..atypical cluster-ligation sequence motif located in the NuoB (NQO6/PSST) subunit rather than in the long advocated NuoI (NQO9/TYKY) subunit...
- Bogachev A, Murtazina R, Skulachev V. H+/e- stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells. J Bacteriol. 1996;178:6233-7 pubmed..These data suggest that (i) the H+/e- stoichiometry for E. coli NDH-I is at least 1.5 and (ii) the DMSO reductase does not generate a proton motive force. ..
- Yagi T, Matsuno Yagi A. The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: the secret unlocked. Biochemistry. 2003;42:2266-74 pubmed
- Erhardt H, Steimle S, Muders V, Pohl T, Walter J, Friedrich T. Disruption of individual nuo-genes leads to the formation of partially assembled NADH:ubiquinone oxidoreductase (complex I) in Escherichia coli. Biochim Biophys Acta. 2012;1817:863-71 pubmed publisher..The inactive population is missing cluster N2 and is tightly associated with the inducible lysine decarboxylase. This article is part of a Special Issue entitled: Biogenesis/Assembly of Respiratory Enzyme Complexes. ..
- Friedrich T, Bottcher B. The gross structure of the respiratory complex I: a Lego System. Biochim Biophys Acta. 2004;1608:1-9 pubmed..This model reflects the evolution of complex I from pre-existing modules for electron transfer and proton translocation. ..
- Falk Krzesinski H, Wolfe A. Genetic analysis of the nuo locus, which encodes the proton-translocating NADH dehydrogenase in Escherichia coli. J Bacteriol. 1998;180:1174-84 pubmed..In particular, we present evidence that NuoG, a peripheral subunit, is essential for complex I function and that it plays a role in the regulation of nuo expression and/or the assembly of complex I. ..
- Sinegina L, Wikstrom M, Verkhovsky M, Verkhovskaya M. Activation of isolated NADH:ubiquinone reductase I (complex I) from Escherichia coli by detergent and phospholipids. Recovery of ubiquinone reductase activity and changes in EPR signals of iron-sulfur clusters. Biochemistry. 2005;44:8500-6 pubmed..895, 1.904, 2.05, which corresponds to the parameters reported for the N2 cluster. This data indicates conformational rearrangements of catalytic importance in complex I upon binding of phospholipids. ..
- Torres Bacete J, Nakamaru Ogiso E, Matsuno Yagi A, Yagi T. Characterization of the NuoM (ND4) subunit in Escherichia coli NDH-1: conserved charged residues essential for energy-coupled activities. J Biol Chem. 2007;282:36914-22 pubmed..The data suggest that these His are not involved in the catalytic Q-binding. Functional roles of NuoM and advantages of NDH-1 research as a model for mitochondrial complex I study have been discussed. ..
- Leif H, Weidner U, Berger A, Spehr V, Braun M, van Heek P, et al. Escherichia coli NADH dehydrogenase I, a minimal form of the mitochondrial complex I. Biochem Soc Trans. 1993;21:998-1001 pubmed
- Steuber J. The C-terminally truncated NuoL subunit (ND5 homologue) of the Na+-dependent complex I from Escherichia coli transports Na+. J Biol Chem. 2003;278:26817-22 pubmed..This Na+ uptake was prevented by EIPA (5-(N-ethyl-N-isopropyl)-amiloride), which acts as inhibitor against Na+/H+ antiporters. ..
- Berrisford J, Thompson C, Sazanov L. Chemical and NADH-induced, ROS-dependent, cross-linking between subunits of complex I from Escherichia coli and Thermus thermophilus. Biochemistry. 2008;47:10262-70 pubmed publisher..Our observations suggest that oxidative damage to complex I in vivo may include not only side-chain modifications but also protein cross-linking and degradation. ..
- Yang Y, Bennett G, San K. Effect of inactivation of nuo and ackA-pta on redistribution of metabolic fluxes in Escherichia coli. Biotechnol Bioeng. 1999;65:291-7 pubmed..Mutations in both ackA-pta and nuo are required to significantly reduce the flux through the PFL pathway. ..
- Steuber J, Schmid C, Rufibach M, Dimroth P. Na+ translocation by complex I (NADH:quinone oxidoreductase) of Escherichia coli. Mol Microbiol. 2000;35:428-34 pubmed..With an E. coli mutant deficient in complex I, the Na+ transport activity was low (1-3 nmol mg-1 min-1), and rotenone was without effect. ..
- Friedrich T, Scheide D. The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases. FEBS Lett. 2000;479:1-5 pubmed..Six of them are also present in a family of membrane-bound multisubunit [NiFe] hydrogenases. It is discussed that they build a module for electron transfer coupled to proton translocation. ..
- Neijssel O, Teixeira de Mattos M. The energetics of bacterial growth: a reassessment. Mol Microbiol. 1994;13:172-82 pubmed..The different strains indeed show different growth efficiencies. The physiological significance of energetically less-efficient branches of the respiratory chain is discussed. ..
- Calhoun M, Gennis R. Demonstration of separate genetic loci encoding distinct membrane-bound respiratory NADH dehydrogenases in Escherichia coli. J Bacteriol. 1993;175:3013-9 pubmed..The enzyme encoded by this locus probably translocates protons across the inner membrane, contributing to the proton motive force. ..
- Kervinen M, Pätsi J, Finel M, Hassinen I. A pair of membrane-embedded acidic residues in the NuoK subunit of Escherichia coli NDH-1, a counterpart of the ND4L subunit of the mitochondrial complex I, are required for high ubiquinone reductase activity. Biochemistry. 2004;43:773-81 pubmed
- Flemming D, Schlitt A, Spehr V, Bischof T, Friedrich T. Iron-sulfur cluster N2 of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB. J Biol Chem. 2003;278:47602-9 pubmed..Complex I from Escherichia coli consists of 13 polypeptides called NuoA to N. Either subunit NuoB or NuoI could harbor Fe/S cluster N2...
- Friedrich T, Weidner U, Nehls U, Fecke W, Schneider R, Weiss H. Attempts to define distinct parts of NADH:ubiquinone oxidoreductase (complex I). J Bioenerg Biomembr. 1993;25:331-7 pubmed..This assumption is further supported by the conserved order of bacterial complex I genes, which correlates with the topological arrangement of the corresponding subunits in the two parts of complex I. ..
- Wackwitz B, Bongaerts J, Goodman S, Unden G. Growth phase-dependent regulation of nuoA-N expression in Escherichia coli K-12 by the Fis protein: upstream binding sites and bioenergetic significance. Mol Gen Genet. 1999;262:876-83 pubmed..This ensures higher ATP yields under conditions where large amounts of ATP are required. ..
- Choice E, Masin D, Bally M, Meloche M, Madden T. Liposomal cyclosporine. Comparison of drug and lipid carrier pharmacokinetics and biodistribution. Transplantation. 1995;60:1006-11 pubmed
- Hayashi M, Miyoshi T, Takashina S, Unemoto T. Purification of NADH-ferricyanide dehydrogenase and NADH-quinone reductase from Escherichia coli membranes and their roles in the respiratory chain. Biochim Biophys Acta. 1989;977:62-9 pubmed..The FAD-containing NQR was very similar to that purified by Jaworowski et al. (Biochemistry (1981) 20, 2041-2047), and reduced Q1 without generating delta psi. ..