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

Molecular Microbiology
A DupuisJ Lunardi

Abstract

Seven out of the 13 proteins encoded by the mitochondrial genome of mammals (peptides ND1 to ND6 plus ND4L) are subunits of the respiratory NADH-ubiquinone oxidoreductase (complex I). The function of these ND subunits is still poorly understood. We have used the NADH-ubiquinone oxidoreductase of Rhodobacter capsulatus as a model for the study of the function of these proteins. In this bacterium, the 14 genes encoding the NADH-ubiquinone oxidoreductase are clustered in the nuo operon. We report here on the biochemical and spectroscopic characterization of mutants individually disrupted in five nuo genes, equivalent to mitochondrial genes nd1, nd2, nd5, nd6 and nd4L. Disruption of any of these genes in R. capsulatus leads to the suppression of NADH dehydrogenase activity at the level of the bacterial membranes and to the disappearance of complex I-associated iron-sulphur clusters. Individual NUO subunits can still be immunodetected in the membranes of these mutants, but they do not form a functional subcomplex. In contrast to these observations, disruption of two ORFs (orf6 and orf7), also present in the distal part of the nuo operon, does not suppress NADH dehydrogenase activity or complex I-associated EPR signals, thus demonstr...Continue Reading

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Citations

Aug 13, 2011·The Journal of Biological Chemistry·Jesus Torres-BaceteTakao Yagi
Jun 25, 2004·Antimicrobial Agents and Chemotherapy·Scott D MillsKathleen MacCormack
Apr 9, 2008·Biochimica Et Biophysica Acta·Daniel SchneiderThorsten Friedrich
Jun 19, 1998·Biochimica Et Biophysica Acta·A DupuisJ P Issartel
Apr 1, 2007·EcoSal Plus·Thorsten Friedrich, Thomas Pohl

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