Inducible transcription of genes involved in taurine uptake and dissimilation by Silicibacter pomeroyi DSS-3T

Gorzynska, Andzelika K.; Denger, Karin; Cook, Alasdair M.; Smits, Theo H. M.

doi:10.1007/s00203-006-0106-8

Cited by 32 publications

(34 citation statements)

References 19 publications

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“…strain 217 (2) and R. pomeroyi DSS-3 (14) utilized (S)-cysteate quantitatively, but neither organism utilized sulfolactate extensively (i.e., ϳ10%). Strains 217 and DSS-3 involve Xsc in taurine metabolism, as observed previously (2,21). Roseobacter sp.…”

Section: Mkat (Kg Protein)supporting

confidence: 76%

Bifurcated Degradative Pathway of 3-Sulfolactate in Roseovarius nubinhibens ISM via Sulfoacetaldehyde Acetyltransferase and ( S )-Cysteate Sulfolyase

et al. 2009

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Data from the genome sequence of the aerobic, marine bacterium Roseovarius nubinhibens ISM were interpreted such that 3-sulfolactate would be degraded as a sole source of carbon and energy for growth via a novel bifurcated pathway including two known desulfonative enzymes, sulfoacetaldehyde acetyltransferase (EC 2.3.3.15) (Xsc) and cysteate sulfo-lyase (EC 4.4.1.25) (CuyA). Strain ISM utilized sulfolactate quantitatively with stoichiometric excretion of the sulfonate sulfur as sulfate. A combination of enzyme assays, analytical chemistry, enzyme purification, peptide mass fingerprinting, and reverse transcription-PCR data supported the presence of an inducible, tripartite sulfolactate uptake system (SlcHFG), and a membrane-bound sulfolactate dehydrogenase (SlcD) which generated 3-sulfopyruvate, the point of bifurcation. 3-Sulfopyruvate was in part decarboxylated by 3-sulfopyruvate decarboxylase (EC 4.1.1.79) (ComDE), which was purified. The sulfoacetaldehyde that was formed was desulfonated by Xsc, which was identified, and the acetyl phosphate was converted to acetyl-coenzyme A by phosphate acetyltransferase (Pta). The other portion of the 3-sulfopyruvate was transaminated to (S)-cysteate, which was desulfonated by CuyA, which was identified. The sulfite that was formed was presumably exported by CuyZ (TC 9.B.7.1.1 in the transport classification system), and a periplasmic sulfite dehydrogenase is presumed. Bioinformatic analyses indicated that transporter SlcHFG is rare but that SlcD is involved in three different combinations of pathways, the bifurcated pathway shown here, via CuyA alone, and via Xsc alone. This novel pathway involves ComDE in biodegradation, whereas it was discovered in the biosynthesis of coenzyme M. The different pathways of desulfonation of sulfolactate presumably represent final steps in the biodegradation of sulfoquinovose (and exudates derived from it) in marine and aquatic environments.Sulfolactate (Fig. 1A) is a widespread natural product, which contains the stable C-SO 3 Ϫ bond. The compound is known to be (i) a component (5% of dry weight) of bacterial endospores (5), (ii) an intermediate in the biosynthesis of coenzyme M in archaea (55), (iii) in equilibrium with (S)-cysteate in mammals (54), (iv) involved in the metabolism of sulfoquinovose (6-deoxy-6-sulfo-D-glucopyranose, the polar moiety of the plant sulfolipid) in plants and algae (e.g., see reference 48), and (v) an intermediate in the bacterial degradation of sulfoquinovose (44).Research on the biodegradation of organosulfonates has concentrated on compounds containing one to four carbon atoms (C 1 , C 2 , C 3 , or C 4 sulfonates), because where appropriate, larger molecules all seemed to be processed via one of the five desulfonative reactions that have been elucidated. Pathways from (i) sulfoquinovose yield, e.g., sulfoacetate or sulfolactate and 2,3-dihydroxy-1-sulfopropane (36, 44), (ii) taurocholate and N-acetyltaurine yield taurine (37, 43), and (iii) N-methyltaurine yield sulfoacetaldehyde (52). The five desulfonatio...

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Section: Mkat (Kg Protein)supporting

confidence: 76%

Bifurcated Degradative Pathway of 3-Sulfolactate in Roseovarius nubinhibens ISM via Sulfoacetaldehyde Acetyltransferase and ( S )-Cysteate Sulfolyase

et al. 2009

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“…The regulator, TauR has been associated with (1) taurine degradative genes since their discovery (e.g., Ruff et al 2003;Brüggemann et al 2004;Denger et al 2006;Gorzynska et al 2006;Baldock et al 2007), with (2) assimilation of taurine nitrogen in R. palustris CGA009 (Denger et al 2004b) (where the same genes [RPB_1035-RPB_1039] are found in R. palustris strains HaA2 and TIE-1), and with (3) assimilation of taurine sulfur, where direct evidence of the function of TauR as a regulatory protein is available (Wiethaus et al 2008). We detected two tauR-like genes (MED92_03198 (tauR2) and MED92_13211 (tauR1)) in the genome of N. caesariensis MED92, and we provisionally annotated the eight open reading frames (ORFs) in the flanking regions ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…1a) is apparently initiated by an ABC transporter for taurine (Table 2, Fig. 4), which is widespread (e.g., Eichhorn et al 2000;Gorzynska et al 2006). There is support for the presence of both Tpa1 and Tpa2 (Table 2).…”

Section: Discussionmentioning

confidence: 99%

“…Previous experience with Tpa in a degradative pathway involved Ald, which released the ammonium ion originating from taurine and apparently allowed release of the ion to the medium via an ammonium-methylammonium transporter (Cook and Denger 2002;Gorzynska et al 2006). Traces of the ammonium ion were detected when taurine served as sole added source of nitrogen for the growth of Klebsiella oxytoca TauN1, which also involves Tpa and Ald .…”

Section: Discussionmentioning

confidence: 99%

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Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: purification of sulfoacetaldehyde dehydrogenase

Krejčík

Denger²,

Weinitschke³

et al. 2008

Arch Microbiol

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Taurine (2-aminoethanesulfonate) is a widespread natural product whose nitrogen moiety was recently shown to be assimilated by bacteria, usually with excretion of an organosulfonate via undefined novel pathways; other data involve transcriptional regulator TauR in taurine metabolism. A screen of genome sequences for TauR with the BLAST algorithm allowed the hypothesis that the marine gammaproteobacterium Neptuniibacter caesariensis MED92 would inducibly assimilate taurine-nitrogen and excrete sulfoacetate. The pathway involved an ABC transporter (TauABC), taurine:pyruvate aminotransferase (Tpa), a novel sulfoacetaldehyde dehydrogenase (SafD) and exporter(s) of sulfoacetate (SafE) (DUF81). Ten candidate genes in two clusters involved three sets of paralogues (for TauR, Tpa and SafE). Inducible Tpa and SafD were detected in cell extracts. SafD was purified 600-fold to homogeneity in two steps. The monomer had a molecular mass of 50 kDa (SDS-PAGE); data from gel filtration chromatography indicated a tetrameric native protein. SafD was specific for sulfoacetaldehyde with a K m -value of 0.12 mM. The N-terminal amino acid sequence of SafD confirmed the identity of the safD gene. The eight pathway genes were transcribed inducibly, which indicated expression of the whole hypothetical pathway. We presume that this pathway is one source of sulfoacetate in nature, where this compound is dissimilated by many bacteria.

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“…Taurine is utilized by environmental bacteria under various metabolic situations (reviewed in reference 6), e.g., as a carbon, nitrogen, and energy source for aerobic heterotrophic growth via the taurine degradation pathway, which has been studied in great detail, including the desulfonation reaction involved (7)(8)(9). At least one bacterium, the marine strain Ruegeria pomeroyi DSS-3, is known to utilize also HT as a source of carbon, nitrogen, and energy (10). However, the HT degradation pathway, and particularly the desulfination reaction involved, remained undefined.…”

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confidence: 99%

Paracoccus denitrificans PD1222 Utilizes Hypotaurine via Transamination Followed by Spontaneous Desulfination To Yield Acetaldehyde and, Finally, Acetate for Growth

et al. 2013

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Hypotaurine (HT; 2-aminoethane-sulfinate) is known to be utilized by bacteria as a sole source of carbon, nitrogen, and energy for growth, as is taurine (2-aminoethane-sulfonate); however, the corresponding HT degradation pathway has remained undefined. Genome-sequenced Paracoccus denitrificans PD1222 utilized HT (and taurine) quantitatively for heterotrophic growth and released the HT sulfur as sulfite (and sulfate) and HT nitrogen as ammonium. Enzyme assays with cell extracts suggested that an HT-inducible HT:pyruvate aminotransferase (Hpa) catalyzes the deamination of HT in an initial reaction step. Partial purification of the Hpa activity and peptide fingerprinting-mass spectrometry (PF-MS) identified the Hpa candidate gene; it encoded an archetypal taurine:pyruvate aminotransferase (Tpa). The same gene product was identified via differential PAGE and PF-MS, as was the gene of a strongly HT-inducible aldehyde dehydrogenase (Adh). Both genes were overexpressed in Escherichia coli. The overexpressed, purified Hpa/Tpa showed HT:pyruvate-aminotransferase activity. Alanine, acetaldehyde, and sulfite were identified as the reaction products but not sulfinoacetaldehyde; the reaction of Hpa/Tpa with taurine yielded sulfoacetaldehyde, which is stable. The overexpressed, purified Adh oxidized the acetaldehyde generated during the Hpa reaction to acetate in an NAD ؉ -dependent reaction. Based on these results, the following degradation pathway for HT in strain PD1222 can be depicted. The identified aminotransferase converts HT to sulfinoacetaldehyde, which desulfinates spontaneously to acetaldehyde and sulfite; the inducible aldehyde dehydrogenase oxidizes acetaldehyde to yield acetate, which is metabolized, and sulfite, which is excreted.

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Inducible transcription of genes involved in taurine uptake and dissimilation by Silicibacter pomeroyi DSS-3T

Cited by 32 publications

References 19 publications

Bifurcated Degradative Pathway of 3-Sulfolactate in Roseovarius nubinhibens ISM via Sulfoacetaldehyde Acetyltransferase and ( S )-Cysteate Sulfolyase

Bifurcated Degradative Pathway of 3-Sulfolactate in Roseovarius nubinhibens ISM via Sulfoacetaldehyde Acetyltransferase and ( S )-Cysteate Sulfolyase

Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: purification of sulfoacetaldehyde dehydrogenase

Paracoccus denitrificans PD1222 Utilizes Hypotaurine via Transamination Followed by Spontaneous Desulfination To Yield Acetaldehyde and, Finally, Acetate for Growth

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