Genomes and Genes
Gene Symbol: nuoJ
Description: NADH:ubiquinone oxidoreductase, membrane subunit J
Alias: ECK2274, JW2275
Species: Escherichia coli str. K-12 substr. MG1655
- 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. ..
- 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. ..
- 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. ..
- 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..Within intact E. coli complex I, the cross-link between the hydrophobic subunits NuoA and NuoJ was abolished in the presence of NADH, indicating that conformational changes extend into the membrane domain, ..
- Mamedova A, Holt P, Carroll J, Sazanov L. Substrate-induced conformational change in bacterial complex I. J Biol Chem. 2004;279:23830-6 pubmed..The enzyme retains its L-shape in the presence of NADH, but exhibits a significantly more open or expanded structure both in the peripheral arm and, unexpectedly, in the membrane domain also. ..
- 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. ..
- 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. ..
- Poole R, Haddock B. Energy-linked reduction of nicotinamide--adenine dinucleotide in membranes derived from normal and various respiratory-deficient mutant strains of Escherichia coli K12. Biochem J. 1974;144:77-85 pubmed..8. Results are interpreted as evidence of the ubiquinone-dependent, but cytochrome-independent, nature of the site I region of the respiratory chain in E. coli. ..
- 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
- Pr ss B, Nelms J, Park C, Wolfe A. Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect growth on mixed amino acids. J Bacteriol. 1994;176:2143-50 pubmed..We propose that cells defective for NADH dehydrogenase I exhibit all these phenotypes, because large NADH/NAD+ ratios inhibit certain tricarboxylic acid cycle enzymes, e.g., citrate synthase and malate dehydrogenase...
- Guenebaut V, Schlitt A, Weiss H, Leonard K, Friedrich T. Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I). J Mol Biol. 1998;276:105-12 pubmed
- 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...
- 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. ..
- 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. ..
- 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
- 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. ..
- 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. ..
- 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. ..
- 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
- 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. ..
- 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. ..
- Euro L, Belevich G, Wikstrom M, Verkhovskaya M. High affinity cation-binding sites in Complex I from Escherichia coli. Biochim Biophys Acta. 2009;1787:1024-8 pubmed publisher..K(+) and La(3+) do not occupy the same site. Possible localization of these metal-binding sites and their implication in catalysis are discussed. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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...
- 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
- 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. ..
- 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. ..
- Yagi T, Matsuno Yagi A. The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: the secret unlocked. Biochemistry. 2003;42:2266-74 pubmed
- 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. ..
- Yagi T. Inhibition by capsaicin of NADH-quinone oxidoreductases is correlated with the presence of energy-coupling site 1 in various organisms. Arch Biochem Biophys. 1990;281:305-11 pubmed..The mechanism by which capsaicin inhibits the energy-transducing NADH-quinone oxidoreductase is discussed. ..
- 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. ..
- 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..Thus, there is no third binuclear iron-sulfur "N1c" in the E. coli complex I but an additional tetranuclear cluster that may be coined N7. ..
- Unden G, Bongaerts J. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim Biophys Acta. 1997;1320:217-34 pubmed..Reductive activation could be achieved by cellular reductants in the absence of O2. In addition, O2 may cause destruction and loss of the FeS cluster. It is not known whether this process is required for regulation of FNR function. ..
- 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. ..
- Bottcher B, Scheide D, Hesterberg M, Nagel Steger L, Friedrich T. A novel, enzymatically active conformation of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). J Biol Chem. 2002;277:17970-7 pubmed..Only the horseshoe-shaped complex I exhibits enzyme activity in detergent solution, which is abolished by the addition of salt. Therefore, it is proposed that this structure is the native conformation of the complex in the membrane. ..
- 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. ..
- Satoh T, Miyoshi H, Sakamoto K, Iwamura H. Comparison of the inhibitory action of synthetic capsaicin analogues with various NADH-ubiquinone oxidoreductases. Biochim Biophys Acta. 1996;1273:21-30 pubmed..1990) Arch. Biochem. Biophys. 281, 305-311). It is noteworthy that several synthetic capsaicins discriminated between NDH-1 and NDH-2 much better than natural capsaicin. ..
- Pohl T, Uhlmann M, Kaufenstein M, Friedrich T. Lambda Red-mediated mutagenesis and efficient large scale affinity purification of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Biochemistry. 2007;46:10694-702 pubmed..After reconstitution in proteoliposomes it couples the electron transfer with proton translocation in an inhibitor sensitive manner, thus meeting all prerequisites for structural and functional studies. ..
- Pätsi J, Kervinen M, Finel M, Hassinen I. Leber hereditary optic neuropathy mutations in the ND6 subunit of mitochondrial complex I affect ubiquinone reduction kinetics in a bacterial model of the enzyme. Biochem J. 2008;409:129-37 pubmed..We have now examined the effects of ND6 mutations on the function of complex I using the homologous NuoJ subunit of Escherichia coli NDH-1 (NADH:quinone oxidoreductase) as a model system...
- Holt P, Morgan D, Sazanov L. 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. 2003;278:43114-20 pubmed..This is consistent with proposals that the mechanism of proton pumping by complex I is likely to involve long range conformational changes. ..
- Finel M, Majander A. Studies on the proton-translocating NADH:ubiquinone oxidoreductases of mitochondria and Escherichia coli using the inhibitor 1,10-phenanthroline. FEBS Lett. 1994;339:142-6 pubmed..EPR spectroscopy of membranous E. coli NDH1 shows that two slow- and one fast-relaxing Fe-S clusters become detectable upon reduction by NADH in the presence of OP. However, none of them resembles the mitochondrial cluster 2. ..
- Matsushita K, Ohnishi T, Kaback H. NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry. 1987;26:7732-7 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. ..
- Verkhovskaya M, Belevich N, Euro L, Wikstrom M, Verkhovsky M. Real-time electron transfer in respiratory complex I. Proc Natl Acad Sci U S A. 2008;105:3763-7 pubmed publisher..Possible consequences of these findings for the proton translocation mechanism are 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. ..
- 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. ..
- 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. ..
- 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..Using the Escherichia coli enzyme (NDH-1), we have investigated the NuoJ subunit (the E. coli counterpart of ND6) by employing a chromosomal DNA manipulation technique...
- Friedrich T. The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochim Biophys Acta. 1998;1364:134-46 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. ..