Regulation of expression of Na + -translocating NADH:quinone oxidoreductase genes in Vibrio harveyi and Klebsiella pneum
- PDF / 333,820 Bytes
- 8 Pages / 595.276 x 790.866 pts Page_size
- 32 Downloads / 224 Views
ORIGINAL PAPER
Regulation of expression of Na+-translocating NADH:quinone oxidoreductase genes in Vibrio harveyi and Klebsiella pneumoniae Maria S. Fadeeva Æ Evgenia A. Yakovtseva Æ Galina A. Belevich Æ Yulia V. Bertsova Æ Alexander V. Bogachev
Received: 2 February 2007 / Revised: 16 March 2007 / Accepted: 28 April 2007 / Published online: 6 June 2007 Springer-Verlag 2007
Abstract The expression of genes encoding sodiumtranslocating NADH:quinone oxidoreductase (Na+-NQR) was studied in the marine bacterium Vibrio harveyi and in the enterobacterium Klebsiella pneumoniae. It has been shown that such parameters as NaCl concentration, pH value, and presence of an uncoupler in the growth media do not influence significantly the level of nqr expression. However, nqr expression depends on the growth substrates used by these bacteria. Na+-NQR is highly repressed in V. harveyi during anaerobic growth, and nqr expression is modulated by electron acceptors and values of their redox potentials. The latter effect was shown to be independent of the ArcAB regulatory system. Keywords Regulation Sodium translocation Na+-NQR NADH dehydrogenase Klebsiella pneumoniae Vibrio ArcB Communicated by David Kelly.
Abbreviations Ap Ampicillin CCCP Carbonyl cyanide m-chlorophenylhydrazone DMSO Dimethyl sulfoxide dNADH Reduced nicotinamide hypoxanthine dinucleotide Km Kanamycin Na+-NQR Na+-translocating NADH:quinone oxidoreductase NDH-1 H+-translocating NADH:quinone oxidoreductase NDH-2 Non-coupled NADH:quinone oxidoreductase NpGal o-nitrophenyl-b-D-galactopyranoside PCR Polymerase chain reaction SBP Sub-bacterial particles Rf Rifampicin Tc Tetracycline TMAO Trimethylamine N-oxide DlNaþ Transmembrane difference in electrochemical potentials of sodium ions.
Accession number: EF394942 (Vibrio harveyi arcB gene, partial cds).
Electronic supplementary material The online version of this article (doi:10.1007/s00203-007-0254-5) contains supplementary material, which is available to authorized users. M. S. Fadeeva E. A. Yakovtseva G. A. Belevich Y. V. Bertsova A. V. Bogachev (&) Department of Molecular Energetics of Microorganisms, A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Leninskie Gory, Moscow, 119992, Russia e-mail: [email protected] Present Address: G. A. Belevich Institute of Biotechnology, University of Helsinki, P.O. Box 65, Viikinkaari 1, 00014 Helsinki, Finland
Introduction NADH can be oxidized by the respiratory chain of bacteria via NADH:quinone oxidoreductases that belong to three different enzyme families having no substantial homology between each other. These are enzymes of NDH-1, NDH-2, and Na+-NQR types. Bacterial NDH-1-type NADH:quinone oxidoreductases are homologous to mitochondrial Complex I. They consist of 13–15 subunits and typically contain 8–9 Fe–S clusters and noncovalently bound FMN as prosthetic groups (Yagi 1991; Ohnishi et al. 1998; Friedrich and Scheide 2000; Hinchliffe and Sazanov 2005). The activity of these en-
123
342 Table 1 Bacterial strains a
Data Loading...
