Genomes and Genes
Gene Symbol: nuoE
Description: NADH:ubiquinone oxidoreductase, chain E
Alias: ECK2279, JW2280
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. ..
- 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. ..
- 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. ..
- Liao P, Choi Y, Lee K. FSscan: a mechanism-based program to identify +1 ribosomal frameshift hotspots. Nucleic Acids Res. 2009;37:7302-11 pubmed publisher..FSscan successfully identified the +1 PRF site in prfB and predicted yehP, pepP, nuoE and cheA as +1 frameshift candidates in the E. coli genome...
- David P, Baumann M, Wikstrom M, Finel M. Interaction of purified NDH-1 from Escherichia coli with ubiquinone analogues. Biochim Biophys Acta. 2002;1553:268-78 pubmed..Both ubiquinone-2 and decylubiquinone are good acceptors for this enzyme, while affinity of NDH-1 for ubiquinone-1 is clearly lower than for the other two, particularly in the purified state. ..
- Matsushita K, Ohnishi T, Kaback H. NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry. 1987;26:7732-7 pubmed
- 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..NADH dehydrogenase fragment has a molecular mass of approximately 170,000 Da and consists of the subunits NuoE, F, and G...
- Ericsson U, Hallberg B, DeTitta G, Dekker N, Nordlund P. Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal Biochem. 2006;357:289-98 pubmed..This suggests that thermofluor constitutes an efficient generic high-throughput method for identification of protein properties predictive of crystallizability. ..
- 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. ..
- 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..It comprises the subunits NuoE, F and G and harbors one flavin mononucleotide and up to six iron-sulfur clusters...
- 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. ..
- 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. ..
- 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. ..
- Friedrich T. The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochim Biophys Acta. 1998;1364:134-46 pubmed
- 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
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- Pohl T, Spatzal T, Aksoyoglu M, Schleicher E, Rostas A, Lay H, et al. Spin labeling of the Escherichia coli NADH ubiquinone oxidoreductase (complex I). Biochim Biophys Acta. 2010;1797:1894-900 pubmed publisher..The distances between the labeled quinone and other complex I variants will be determined in future experiments to receive further geometry information by triangulation. ..
- 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. ..
- 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. ..
- 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
- 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. ..
- 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
- 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. ..
- 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. ..
- 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. ..
- 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
- 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...
- 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. ..
- 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. ..
- Ohnishi T. Iron-sulfur clusters/semiquinones in complex I. Biochim Biophys Acta. 1998;1364:186-206 pubmed..A brief introduction of EPR technique was also described in Appendix A of this mini-review. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- Uhlmann M, Friedrich T. EPR signals assigned to Fe/S cluster N1c of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) derive from cluster N1a. Biochemistry. 2005;44:1653-8 pubmed..soluble NADH dehydrogenase fragment represents the electron input part of the complex and consists of the subunits NuoE, F, and G. The FMN and four iron-sulfur clusters have been detected in this fragment by means of EPR spectroscopy...
- Kabir M, Shimizu K. Metabolic regulation analysis of icd-gene knockout Escherichia coli based on 2D electrophoresis with MALDI-TOF mass spectrometry and enzyme activity measurements. Appl Microbiol Biotechnol. 2004;65:84-96 pubmed..activity significantly affected the respiratory system and electron transport chain, as evidenced by the significant downregulation of proteins encoded by the genes nuoE, nuoH, cydA and cyoA in icd mutant E. coli compared to the parent.
- 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. ..
- 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
- 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. ..