Distal genes of the <i>nuo</i> operon of <i>Rhodobacter capsulatus</i> equivalent to the mitochondrial ND subunits are all essential for the biogenesis of the respiratory NADH–ubiquinone oxidoreductase

Dupuis, Alain; Darrouzet, Élisabeth; Duborjal, H.; Pierrard, Béatrice; Chevallet, Mireille; Belzen, R. van; Albracht, S.P.J.; Lunardi, Joël

doi:10.1046/j.1365-2958.1998.00814.x

Cited by 28 publications

(24 citation statements)

References 41 publications

(52 reference statements)

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“…Nakamaru-Ogiso et al (25) described the presence of small inactive NDH-1 subcomplexes when the NuoL-KO membrane was analyzed by BN-PAGE. Quite similar results were reported by Dupuis et al (45,46) who described a deficit of NDH-1 activity and assembly in membranes vesicles of the NuoL knock-out mutant from Rhodobacter capsulatus. Furthermore, it was described that the deletion of the homologue MrpA subunit from the Na ϩ /H ϩ antiporter from Bacillus subtilis results into complete loss of activity (47,48).…”

Section: Discussionsupporting

confidence: 87%

Structural Contribution of C-terminal Segments of NuoL (ND5) and NuoM (ND4) Subunits of Complex I from Escherichia coli

Torres‐Bacete

Sinha

Matsuno‐Yagi

et al. 2011

Journal of Biological Chemistry

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The proton-translocating NADH-quinone oxidoreductase (complex I/NDH-1) is a multisubunit enzymatic complex. It has a characteristic L-shaped form with two domains, a hydrophilic peripheral domain and a hydrophobic membrane domain. The membrane domain contains three antiporter-like subunits (NuoL, NuoM, and NuoN, Escherichia coli naming) that are considered to be involved in the proton translocation. Deletion of either NuoL or NuoM resulted in an incomplete assembly of NDH-1 and a total loss of the NADH-quinone oxidoreductase activity. We have truncated the C terminus segments of NuoM and NuoL by introducing STOP codons at different locations using site-directed mutagenesis of chromosomal DNA. Our results suggest an important structural role for the C-terminal segments of both subunits. The data further advocate that the elimination of the last transmembrane helix (TM14) of NuoM and the TM16 (at least C-terminal seven residues) or together with the HL helix and the TM15 of the NuoL subunit lead to reduced stability of the membrane arm and therefore of the whole NDH-1 complex. A region of NuoL critical for stability of NDH-1 architecture has been discussed.

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Section: Discussionsupporting

confidence: 87%

Structural Contribution of C-terminal Segments of NuoL (ND5) and NuoM (ND4) Subunits of Complex I from Escherichia coli

Torres‐Bacete

Sinha

Matsuno‐Yagi

et al. 2011

Journal of Biological Chemistry

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“…An insertional mutant in a putative NADH : ubiquinone oxidoreductase gene grew normally on methanol and showed impaired growth on succinate and pyruvate. A similar heterotrophic phenotype of NADH : ubiquinone oxidoreductase mutants has been observed in Rhodobacter capsulatus, with impaired aerobic growth on malate and succinate (Dupuis et al, 1998).…”

Section: Discussionsupporting

confidence: 68%

Reconstruction of C3 and C4 metabolism in Methylobacterium extorquens AM1 using transposon mutagenesis

et al. 2003

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The growth of Methylobacterium extorquens AM1 on C 1 compounds has been well-studied, but little is known about how this methylotroph grows on multicarbon compounds. A Tn5 transposon mutagenesis procedure was performed to identify genes involved in the growth of M. extorquens AM1 on succinate and pyruvate. Of the 15 000 insertion colonies screened, 71 mutants were found that grew on methanol but either grew slowly or were unable to grow on one or both of the multicarbon substrates. For each of these mutants, the chromosomal region adjacent to the insertion site was sequenced, and 55 different genes were identified and assigned putative functions. These genes fell into a number of predicted categories, including central carbon metabolism, carbohydrate metabolism, regulation, transport and non-essential housekeeping functions. This study focused on genes predicted to encode enzymes of central heterotrophic metabolism: 2-oxoglutarate dehydrogenase, pyruvate dehydrogenase and NADH : ubiquinone oxidoreductase. In each case, the mutants showed normal growth on methanol and impaired growth on pyruvate and succinate, consistent with a role specific to heterotrophic metabolism. For the first two cases, no detectable activity of the corresponding enzyme was found in the mutant, verifying the predictions. The results of this study were used to reconstruct multicarbon metabolism of M. extorquens AM1 during growth on methanol, succinate and pyruvate.

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“…Due to its complexity, complex I is the least-understood component of the various known respiratory complexes. Only the R. capsulatus complex I was shown to readily reverse electron flow between the quinone pool and NAD ϩ (7,9).…”

mentioning

confidence: 99%

Complex I and Its Involvement in Redox Homeostasis and Carbon and Nitrogen Metabolism in Rhodobacter capsulatus

2001

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A transposon mutant of Rhodobacter capsulatus, strain Mal7, that was incapable of photoautotrophic and chemoautotrophic growth and could not grow photoheterotrophically in the absence of an exogenous electron acceptor was isolated. The phenotype of strain Mal7 suggested that the mutation was in some gene(s) not previously shown to be involved in CO(2) fixation control. The site of transposition in strain Mal7 was identified and shown to be in the gene nuoF, which encodes one of the 14 subunits for NADH ubiquinone-oxidoreductase, or complex I. To confirm the role of complex I and nuoF for CO(2)-dependent growth, a site-directed nuoF mutant was constructed (strain SBC1) in wild-type strain SB1003. The complex I-deficient strains Mal7 and SBC1 exhibited identical phenotypes, and the pattern of CO(2) fixation control through the Calvin-Benson-Bassham pathway was the same for both strains. It addition, it was shown that electron transport through complex I led to differential control of the two major cbb operons of this organism. Complex I was further shown to be linked to the control of nitrogen metabolism during anaerobic photosynthetic growth of R. capsulatus.

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Distal genes of the nuo operon of Rhodobacter capsulatus equivalent to the mitochondrial ND subunits are all essential for the biogenesis of the respiratory NADH–ubiquinone oxidoreductase

Cited by 28 publications

References 41 publications

Structural Contribution of C-terminal Segments of NuoL (ND5) and NuoM (ND4) Subunits of Complex I from Escherichia coli

Structural Contribution of C-terminal Segments of NuoL (ND5) and NuoM (ND4) Subunits of Complex I from Escherichia coli

Reconstruction of C3 and C4 metabolism in Methylobacterium extorquens AM1 using transposon mutagenesis

Complex I and Its Involvement in Redox Homeostasis and Carbon and Nitrogen Metabolism in Rhodobacter capsulatus

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