delta-Aminolevulinic acid dehydratase deficiency can cause delta-aminolevulinate auxotrophy in Escherichia coli

O’Neill, Gary P.; Thorbjarnardóttir, Sigrídur H.; Michelsen, Uwe; Palsson, Stefan; Söll, Dieter; Eggertsson, Guðmundur

doi:10.1128/jb.173.1.94-100.1991

Cited by 11 publications

(7 citation statements)

References 41 publications

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“…As shown above, the majority of the insertions in our placMu9 mutants expressing ␤-galactosidase under sulfate starvation conditions were clustered in the region at 8.5 min on the chromosome, downstream of the hemB gene. This region is contained on plasmid pUC18ALA4 (37). The nucleotide sequence of the 3,682-bp NsiI-HpaI fragment immediately downstream of hemB was determined (Fig.…”

Section: Resultsmentioning

confidence: 99%

Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source

et al. 1996

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Genes whose expression is regulated by sulfate starvation in Escherichia coli were identified by generating random translational lacZ fusions in the chromosome with the placMu9 system. Nine lacZ fusion strains which expressed ␤-galactosidase after growth under sulfate starvation conditions but not after growth in the presence of sulfate were found. These included two strains with insertions in the dmsA and rhsD genes, respectively, and seven strains in which the insertions were located within a 1.8-kb region downstream of hemB at 8.5 minutes on the E. coli chromosome. Analysis of the nucleotide sequence of this region indicated the presence of four open reading frames designated tauABCD. Disruption of these genes resulted in the loss of the ability to utilize taurine (2-aminoethanesulfonate) as a source of sulfur but did not affect the utilization of a range of other aliphatic sulfonates as sulfur sources. The TauA protein contained a putative signal peptide for transport into the periplasm; the TauB and TauC proteins showed sequence similarity to ATP-binding proteins and membrane proteins, respectively, of ABC-type transport systems; and the TauD protein was related in sequence to a dichlorophenoxyacetic acid dioxygenase. We therefore suggest that the proteins encoded by tauABC constitute an uptake system for taurine and that the product of tauD is involved in the oxygenolytic release of sulfite from taurine. The transcription initiation site was detected 26 to 27 bp upstream of the translational start site of tauA. Expression of the tauD gene was dependent on CysB, the transcriptional activator of the cysteine regulon.

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Section: Resultsmentioning

confidence: 99%

Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source

et al. 1996

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“…In addition, one mutant which requires both ALA and cysteine was found. With one exception, the Ala-mutants grew well on L agar supplemented with ALA and therefore do not belong to the class of ALA-requiring hemB mutants recently described (31). All Ala-mutants had a leaky phenotype.…”

Section: Methodsmentioning

confidence: 99%

The Escherichia coli hemL gene encodes glutamate 1-semialdehyde aminotransferase

et al. 1991

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“…First, an NdeI site at the translation start of tauD was introduced by polymerase chain reaction amplification of the tauD gene from plasmid pUC18ALA4 (2,10). The oligonucleotide primers used were EE1 (5Ј-CATGGAGAAGT-CATATGAGTGAAC-3Ј, with the change to introduce the NdeI site underlined) and EE2 (5Ј-CGGTGCTCGAAAGCTTAGGTTCGA-3Ј).…”

Section: Methodsmentioning

confidence: 99%

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

Eichhorn

Ploeg

Kertesz

et al. 1997

Journal of Biological Chemistry

250

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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delta-Aminolevulinic acid dehydratase deficiency can cause delta-aminolevulinate auxotrophy in Escherichia coli

Cited by 11 publications

References 41 publications

Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source

Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source

The Escherichia coli hemL gene encodes glutamate 1-semialdehyde aminotransferase

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

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