Sulphonate utilization by enteric bacteria

Uria-Nickelsen, Maria; Leadbetter, Edward R.; Godchaux, Walter

doi:10.1099/00221287-139-2-203

Cited by 53 publications

(53 citation statements)

References 12 publications

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“…Recognition of the regulation of metabolism of organosulfonates is not new (20)(21)(22), but we now conclude that a global regulatory network is involved (sulfate starvation-induced stimulon, SSIS) (8,23), and this has yet to be evaluated as an ecological phenomenon. The potential ecological relevance of the network should be considered together with the growing awareness of the extent of pollution by sulfonated compounds (e.g.…”

Section: R-ch 2 -Somentioning

confidence: 99%

Bacterial Desulfonation of the Ethanesulfonate Metabolite of the Chloroacetanilide Herbicide Metazachlor

Laue

Field

Cook

1996

Environ. Sci. Technol.

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Metazachlor (R-CH 2 -Cl), a chloroacetanilide herbicide, is converted in soil to products including the ethanesulfonate metabolite (R-CH 2 -SO 3 -; BH 479-8). Nothing is known about the degradation of the ethanesulfonates of this class of herbicides. We used inocula derived from five sources for enrichment cultures to utilize R-CH 2 -SO 3 -as a sole sulfur source for the growth of microorganisms. Each culture yielded bacteria that caused the disappearance of R-CH 2 -SO 3 -and the formation of a product identified as the glycolate metabolite (R-CH 2 -OH; BH 479-1) by mass spectrometry. A pure culture, strain HL1, was isolated, and this bacterium quantitatively desulfonated R-CH 2 -SO 3 -, the sulfur being recovered in cell protein. Recovery of the organic moiety was usually about 80%. A second ethanesulfonate (R′-CH 2 -SO 3 -) and two alkylsulfonates, but not taurine, were utilized by strain HL1 as sulfur sources.

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Section: R-ch 2 -Somentioning

confidence: 99%

Bacterial Desulfonation of the Ethanesulfonate Metabolite of the Chloroacetanilide Herbicide Metazachlor

Laue

Field

Cook

1996

Environ. Sci. Technol.

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“…Expression of the tauD gene was shown to depend on functional CysB, and it was fully repressed in the presence of cysteine or cystine and also during growth with sulfate (37). Utilization of sulfate-sulfur in preference to taurine-sulfur (36) is thus due to repression of tauABCD expression in the presence of sulfate.…”

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confidence: 96%

“…Sulfonate sulfur is of particular interest, as it accounts for over 40% of the total sulfur in the soil (2) and is also released into the environment in the form of man-made pollutants (20). E. coli is able to utilize several aliphatic sulfonates as sulfur sources (36,37). During growth with ethanesulfonate or glutathione, the organism produces a set of proteins which are absent during growth with either cysteine or sulfate (21,30).…”

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confidence: 99%

Involvement of CysB and Cbl regulatory proteins in expression of the tauABCD operon and other sulfate starvation-inducible genes in Escherichia coli

et al. 1997

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Starvation for sulfate results in increased synthesis of several proteins in Escherichia coli. Among these Ssi (sulfate starvation-induced) proteins are the products of the tauABCD genes, which are required for utilization of taurine as sulfur source for growth. In this study, the role of the cbl gene in expression of tauABCD and other ssi genes was investigated. The protein encoded by cbl shows high sequence similarity to CysB, the LysR-type transcriptional activator of the genes involved in cysteine biosynthesis. Strain EC2541, which contains an internal deletion in cbl, was unable to utilize taurine and other aliphatic sulfonates as sulfur sources. Two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that many of the Ssi proteins were not synthesized in EC2541. Expression of a translational tauD-lacZ fusion required the presence of both cbl and cysB. The interactions of CysB and Cbl with the promoter region of tauABCD were studied by using gel mobility shift experiments and DNase I footprinting. CysB occupied multiple binding sites, whereas Cbl occupied only one site from 112 to 68 bp upstream of the transcription start site. Acetylserine, the inducer of transcription of CysB-regulated genes, stimulated binding of CysB but not of Cbl. Sulfate had no effect on binding of both proteins to the tauABCD promoter region. These results indicate that Cbl is a transcription factor for genes required for sulfonate-sulfur utilization and maybe for other genes whose expression is induced by sulfate starvation.Cysteine biosynthesis via sulfate assimilation in plants and microorganisms represents the predominant mechanism by which inorganic sulfur is reduced and incorporated into organic compounds. This pathway has been characterized in detail in Escherichia coli and Salmonella typhimurium (see reference 24 for a recent review). Most of the genes involved are coordinately regulated as the cysteine regulon-high-level expression of these genes requires sulfur limitation, the LysRtype (11, 34) transcriptional regulator CysB, and the presence of the inducer molecule N-acetyl-L-serine. Transcription from cys gene promoters is initiated by CysB protein binding to activation sites positioned just upstream of the Ϫ35 regions of these promoters, and inducer facilitates interaction of CysB with these sites (15,23,28). Sulfur limitation is a necessary condition for derepression of the cys regulon because L-cysteine inhibits the serine transacetylase enzyme required for inducer synthesis. In addition, sulfide and thiosulfate act as anti-inducers of CysB-dependent transcription (13, 23). Maximal expression of cys genes is seen during growth with limiting sulfur sources such as glutathione or L-djenkolic acid, whereas growth with sulfate, sulfite, or thiosulfate leads to partial repression of these genes, and they are fully repressed during growth with sulfide, L-cysteine, and L-cystine (22,24). The partial repression of cys gene expression by sulfate is ascribed to the inhibitory effect of sulfide generated ...

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“…Sulfonates known to provide sulfur include ethanesulfonate, butanesulfonate, L-cysteate, isethionate (2-hydroxyethanesulfonate), and taurine (2-aminoethanesulfonate) (1,2). None of these sulfonates served as sulfur source under anaerobic conditions, nor could they be utilized as a source of carbon and energy or of carbon, energy, and sulfur under either aerobic or anaerobic conditions (1). The mechanisms of sulfur assimilation from aliphatic sulfonates are unknown, but it has been shown that sulfonate/sulfur enters the assimilatory sulfate reduction pathway at the stage of sulfite (3).…”

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confidence: 99%

Characterization of α-Ketoglutarate-dependent Taurine Dioxygenase from Escherichia coli

Eichhorn

Ploeg

Kertesz

et al. 1997

Journal of Biological Chemistry

245

288

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The Escherichia coli tauD gene is required for the utilization of taurine (2-aminoethanesulfonic acid) as a sulfur source and is expressed only under conditions of sulfate starvation. The sequence relatedness of the TauD protein to the ␣-ketoglutarate-dependent 2,4-dichlorophenoxyacetate dioxygenase of Alcaligenes eutrophus suggested that TauD is an ␣-ketoglutarate-dependent dioxygenase catalyzing the oxygenolytic release of sulfite from taurine (van der Ploeg, J. R., Weiss, M. A., Saller, E., Nashimoto, H., Saito, N., Kertesz, M. A., and Leisinger, T. (1996) J. Bacteriol. 178, 5438 -5446). TauD was overexpressed in E. coli to ϳ70% of the total soluble protein and purified to apparent homogeneity by a simple two-step procedure. The apparent M r of 81,000 of the native protein and the subunit M r of 37,400 were consistent with a homodimeric structure. The pure enzyme converted taurine to sulfite and aminoacetaldehyde, which was identified by high pressure liquid chromatography after enzymatic conversion to ethanolamine. The reaction also consumed equimolar amounts of oxygen and ␣-ketoglutarate; ferrous iron was absolutely required for activity; and ascorbate stimulated the reaction. The properties and amino acid sequence of this enzyme thus define it as a new member of the ␣-ketoglutarate-dependent dioxygenase family. The pure enzyme showed maximal activity at pH 6.9 and retained activity on storage at ؊20°C for several weeks. Taurine (K m ‫؍‬ 55 M) was the preferred substrate, but pentanesulfonic acid, 3-(N-morpholino)propanesulfonic acid, and 1,3-dioxo-2-isoindolineethanesulfonic acid were also desulfonated at significant rates. Among the cosubstrates tested, only ␣-ketoglutarate (K m ‫؍‬ 11 M) supported significant dioxygenase activity.In the absence of sulfate, Escherichia coli can utilize aliphatic sulfonates as sulfur sources for growth. Sulfonates known to provide sulfur include ethanesulfonate, butanesulfonate, L-cysteate, isethionate (2-hydroxyethanesulfonate), and taurine (2-aminoethanesulfonate) (1, 2). None of these sulfonates served as sulfur source under anaerobic conditions, nor could they be utilized as a source of carbon and energy or of carbon, energy, and sulfur under either aerobic or anaerobic conditions (1). The mechanisms of sulfur assimilation from aliphatic sulfonates are unknown, but it has been shown that sulfonate/sulfur enters the assimilatory sulfate reduction pathway at the stage of sulfite (3).Recently, we have identified the tauABCD gene cluster, located at 8.5 min on the E. coli chromosome, which is specifically involved in the utilization of taurine as a sulfur source (2). Disruption of tauB, tauC, or tauD resulted in the loss of the ability to utilize taurine as a source of sulfur, but did not affect the utilization of a range of other aliphatic sulfonates as sulfur sources. The tau genes were only expressed during growth in the absence of sulfate or cysteine (2). The amino acid sequences of TauABC exhibit similarity to components of ABC-type transport systems (4). TauA has a p...

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Sulphonate utilization by enteric bacteria

Cited by 53 publications

References 12 publications

Bacterial Desulfonation of the Ethanesulfonate Metabolite of the Chloroacetanilide Herbicide Metazachlor

Bacterial Desulfonation of the Ethanesulfonate Metabolite of the Chloroacetanilide Herbicide Metazachlor

Involvement of CysB and Cbl regulatory proteins in expression of the tauABCD operon and other sulfate starvation-inducible genes in Escherichia coli

Characterization of α-Ketoglutarate-dependent Taurine Dioxygenase from Escherichia coli

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