title: Genome-enabled analysis of the utilization of taurine as sole source of carbon or of nitrogen by Rhodobacter sphaeroides 2.4.1.
abstract: A degradative pathway for taurine (2-aminoethanesulfonate) in Rhodobacter sphaeroides 2.4.1 was proposed by Brüggemann et al. (2004) (Microbiology 150, 805-816) on the basis of a partial genome sequence. In the present study, R. sphaeroides 2.4.1 was found to grow exponentially with taurine as the sole source of carbon and energy for growth. When taurine was the sole source of nitrogen in succinate-salts medium, the taurine was rapidly degraded, and most of the organic nitrogen was excreted as the ammonium ion, which was then utilized for growth. Most of the enzymes involved in dissimilation, taurine dehydrogenase (TDH), sulfoacetaldehyde acetyltransferase (Xsc) and phosphate acetyltransferase (Pta), were found to be inducible, and evidence for transcription of the corresponding genes (tauXY, xsc and pta), as well as of tauKLM, encoding the postulated TRAP transporter for taurine, and of tauZ, encoding the sulfate exporter, was obtained by reverse-transcription PCR. An additional branch of the pathway, observed by Novak et al. (2004) (Microbiology 150, 1881-1891) in R. sphaeroides TAU3, involves taurine : pyruvate aminotransferase (Tpa) and a presumptive ABC transporter (NsbABC). No evidence for a significant role of this pathway, or of the corresponding alanine dehydrogenase (Ald), was obtained for R. sphaeroides 2.4.1. The anaplerotic pathway needed under these conditions in R. sphaeroides 2.4.1 seems to involve malyl-CoA lyase, which was synthesized inducibly, and not malate synthase (GlcB), whose presumed gene was not transcribed under these conditions.
authors.affiliation: Department of Biology, The University, D-78457 Konstanz, Germany.
authors.forename: Karin
authors.initials: K
authors.lastname: Denger
authors.affiliation: Department of Biology, The University, D-78457 Konstanz, Germany.
authors.forename: Theo H M
authors.initials: THM
authors.lastname: Smits
authors.affiliation: Department of Biology, The University, D-78457 Konstanz, Germany.
authors.forename: Alasdair M
authors.initials: AM
authors.lastname: Cook
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000378:metabolism; D000079:Acetaldehyde / Q000031:analogs & derivatives; D000123:Acetyltransferases / Q000235:genetics / Q000378:metabolism; D050788:Alanine Dehydrogenase / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D002244:Carbon / Q000378:metabolism*; D003470:Culture Media; D005798:Genes, Bacterial / Q000235:genetics; D008292:Malate Synthase / Q000378:metabolism; D005810:Multigene Family / Q000235:genetics; D009584:Nitrogen / Q000378:metabolism*; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000235:genetics / Q000378:metabolism; D007652:Oxo-Acid-Lyases / Q000235:genetics / Q000378:metabolism; D010710:Phosphates; D016133:Polymerase Chain Reaction; D019289:Pyruvic Acid; D012242:Rhodobacter sphaeroides / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D019802:Succinic Acid; D013654:Taurine / Q000378:metabolism*; D014158:Transcription, Genetic
chemical_list: D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D003470:Culture Media; D010710:Phosphates; D013654:Taurine; C015517:sulfoacetaldehyde; D002244:Carbon; D019289:Pyruvic Acid; D019802:Succinic Acid; D050788:Alanine Dehydrogenase; C053682:taurine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors; D000123:Acetyltransferases; D008292:Malate Synthase; D007652:Oxo-Acid-Lyases; C021536:malyl-CoA lyase; D000079:Acetaldehyde; D009584:Nitrogen