A five-gene cluster involved in utilization of taurine-nitrogen and excretion of sulfoacetaldehyde by Acinetobacter radi
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ORIGINAL PAPER
A five-gene cluster involved in utilization of taurine-nitrogen and excretion of sulfoacetaldehyde by Acinetobacter radioresistens SH164 Zdene˘k Krejcˇ´ık • David Schleheck • Klaus Hollemeyer • Alasdair M. Cook
Received: 1 August 2011 / Revised: 23 January 2012 / Accepted: 15 March 2012 / Published online: 16 May 2012 Ó Springer-Verlag 2012
Abstract Acinetobacter calcoaceticus SW1, under nitrogen limitation, assimilates the nitrogen moiety of taurine (2-aminoethanesulfonate) inducibly and excretes sulfoacetaldehyde, a product of taurine dehydrogenase (TauXY). BLAST searches of newly available genome sequences using the TauXY sequences revealed a 5-gene cluster, tauRXYPI, in Acinetobacter radioresistens SH164. We hypothesized that tauXYPI (HMPREF0018_00717– HMPREF0018_00720) encodes proteins that are orthologs of the undefined pathway from strain SW1, and that tauR (HMPREF0018_00716) encodes the relevant transcriptional regulator. Strain SH164 excreted sulfoacetaldehyde from taurine during growth. TauXY activity was expressed inducibly. Reverse transcription PCR showed that the tauRXYPI genes were transcribed inducibly. This allowed the conclusions that (i) TauP (currently annotated as permease GabP [TC 2.A.3]) is a taurine permease, and (ii)
TauI (currently annotated as DUF6 drug/metabolite exporter [TC 2.A.7]) is a sulfoacetaldehyde exporter. The presumably equifunctional cluster tauRXYPI was then found in strain SW1. TauP is the third recognized taurine uptake system, and TauI is the third postulated class of sulfonate exporters, in bacteria. Keywords Acinetobacter spp. Assimilation of taurine-nitrogen Excretion of sulfoacetaldehyde Novel taurine permease Novel sulfoacetaldehyde exporter Abbreviations RT-PCR Reverse transcription PCR TauABC ABC transporter for taurine tauI Encodes sulfoacetaldehyde exporter tauP Encodes taurine permease tauR Encodes transcriptional regulator of taurine genes tauXY Encode taurine dehydrogenase
Communicated by Ursula Priefer.
Electronic supplementary material The online version of this article (doi:10.1007/s00203-012-0806-1) contains supplementary material, which is available to authorized users. Z. Krejcˇ´ık D. Schleheck A. M. Cook (&) Department of Biology, University of Konstanz, 78457 Constance, Germany e-mail: [email protected] Present Address: Z. Krejcˇ´ık Department of Molecular Genetics, Institute of Hematology and Blood Transfusion, 12820 Prague 2, Czech Republic K. Hollemeyer Institute of Biochemical Engineering, University of the Saarland, 66041 Saarbru¨cken, Germany
Introduction Taurine (2-aminoethanesulfonate) is a major solute, and sometimes an osmolyte, in mammals, fish, red algae and marine creatures, and it is known as a carbon and energy source for terrestrial, freshwater and marine bacteria (e.g. Jones 1953; Allen and Garrett 1971; Kondo et al. 1971; Ito et al. 1977; Huxtable 1992; Yin et al. 2000; Gonza´lez et al. 2003; Ro¨sch et al. 2008). Further, the compound is known as a sulfur source for the growth of bacteria (E
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