TeiR, a LuxR-Type Transcription Factor Required for Testosterone Degradation in<i>Comamonas testosteroni</i>

Pruneda‐Paz, Jose L.; Linares, Mauricio; Cabrera, Julio E.; Genti-Raimondi, Susana

doi:10.1128/jb.186.5.1430-1437.2004

Cited by 40 publications

(33 citation statements)

References 42 publications

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“…Most of the genes in this cluster are involved in aromatization and following degradation of the A-ring in steroid degradation [14] (Figure 11). testosteroni [17,[67][68][69]. This transcriptional regulator is a LuxR family protein and possesses helix-turn-helix motif at the C-terminal to bind DNA.…”

Section: -6 Aromatization Of the A-ring Accompanied By The Cleavagementioning

confidence: 99%

“…This transcriptional regulator is a LuxR family protein and possesses helix-turn-helix motif at the C-terminal to bind DNA. It is an activator which induces 3,17-hsd, 3-hsd, ksi, TesA2 to ORF18-encoded enzyme, TesA1 to TesG, SteA to ORF6-encoded enzyme, the meta-cleavage enzyme and the ORFs in the downstream DNA region [17,67] Homology search for putative steroid degradation genes in the genomic sequence data on the web using deduced amino acid sequences of tesB to ORF33 revealed the presence of putative steroid degradation gene clusters similar to tesB to ORF33 in bacteria of different genera. Among a number of candidate bacteria, ten strains of seven genera were selected for comparison (C. testosteroni CNB-1 [29], C. testosteroni KF1 (draft sequence, accession: NZ_AAUJ02000001) [70,71], Cupriavidu necator (formally R. eutropha) JMP134 (accession: NC_007347) [72,73], Ralstonia eutropha H16 (accession: NC_008314) [74], Burkholderia cenocepacia J2315 (accession: NC_011001) [75], Burkholderia sp.…”

Section: -6 Aromatization Of the A-ring Accompanied By The Cleavagementioning

confidence: 99%

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Steroid degradation in Comamonas testosteroni

Horinouchi

Hayashi

Kudo

2012

The Journal of Steroid Biochemistry and Molecular Biology

114

153

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Steroid degradation by Comamonas testosteroni and Nocardia restrictus have been intensively studied for the purpose of obtaining materials for steroid drug synthesis. C. testosteroni degrades side chains and converts single/double bonds of certain steroid compounds to produce androsta-1,4-diene 3,17-dione or the derivative. Following 9-hydroxylation leads to aromatization of the A-ring accompanied by cleavage of the B-ring, and aromatized A-ring is hydroxylated at C-4 position, cleaved at ∆4 by meta-cleavage, and divided into 2-hydroxyhexa-2,4-dienoic acid (A-ring) and 9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oic acid (B,C,D-ring) by hydrolysis.Reactions and the genes involved in the cleavage and the following degradation of the A-ring are similar to those for bacterial biphenyl degradation, and 9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oic acid degradation is suggested to be mainly -oxidation. Genes involved in A-ring aromatization and degradation form a gene cluster, and the genes involved in -oxidation of 9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oic acid also comprise a large cluster of more than 10 genes. The DNA region between these two main steroid degradation gene clusters contain 3-hydroxysteroid dehydrogenase gene, ∆5,3-ketosteroid isomerase gene, genes for inversion of an -oriented-hydroxyl group to a -oriented-hydroxyl group at C-12 position of cholic acid, and genes possibly involved in the degradation of a side chain at C-17 position of cholic acid, indicating this DNA region of more than 100kb to be a steroid degradation gene hot spot of C. testosteroni.

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Section: -6 Aromatization Of the A-ring Accompanied By The Cleavagementioning

confidence: 99%

Section: -6 Aromatization Of the A-ring Accompanied By The Cleavagementioning

confidence: 99%

Steroid degradation in Comamonas testosteroni

Horinouchi

Hayashi

Kudo

2012

The Journal of Steroid Biochemistry and Molecular Biology

114

153

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“…Cloning of the teiR Gene from C. testosteroni and Subcloning of teiR Gene Fragments-The teiR gene was cloned from C. testosteroni (ATCC 11996) chromosomal DNA by using the following pair of primers: forward primer 5Ј-CGAGCTCCAT-CGCTTGCGTG-3Ј and reverse primer 5Ј-GCGGCCGCTCT-ATGCCCG-3Ј (30). The full teiR gene was then cloned into pCR2.1-TOPO to yield plasmid pTOPO4, which after sequence confirmation (MWG) was used as template for further PCR reactions (Fig.…”

Section: Methodsmentioning

confidence: 99%

“…Repressor B (RepB) turned out to bind to the mRNA of 3␣-HSD/CR, thereby interfering with hsdA translation (29). By transposon mutagenesis, teiR (testosterone-inducible regulator) was identified, a gene that was hypothesized to encode a positive regulator of steroid degradation in C. testosteroni ATCC11996 in the presence of testosterone (30). A similar positive regulator (TesR) was cloned and postulated to regulate a steroid degradation gene clusters in C. testosteroni TA441 (14).…”

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confidence: 99%

Testosterone-inducible Regulator Is a Kinase That Drives Steroid Sensing and Metabolism in Comamonas testosteroni

Göhler¹,

Guan²,

Paulsen³

et al. 2008

Journal of Biological Chemistry

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The mechanism of gene regulation by steroids in bacteria is still a mystery. We use steroid-inducible 3␣-hydroxysteroid dehydrogenase/carbonyl reductase (3␣-HSD/CR) as a reporter system to study steroid signaling in Comamonas testosteroni. In previous investigations we cloned and characterized the 3␣-HSD/CR-encoding gene, hsdA. In addition, we identified two negative regulator genes (repA and repB) in the vicinity of hsdA, the protein products which repress hsdA expression on the level of transcription and translation, respectively. Recently, a positive regulator of hsdA expression, TeiR (testosterone-inducible regulator), was found by transposon mutagenesis, but the mode of its action remained obscure. In the present work we produced a TeiR-green fluorescent fusion protein and showed that TeiR is a membrane protein with asymmetrical localization at one of the cell poles of C. testosteroni. Knock-out mutants of the teiR gene revealed that TeiR provides swimming and twitching motility of C. testosteroni to the steroid substrate source. TeiR also mediated an induced expression of 3␣-HSD/CR which was paralleled by an enhanced catabolism of testosterone. We also found that TeiR responds to a variety of different steroids other than testosterone. Biochemical analysis with several deletion mutants of the teiR gene revealed TeiR to consist of three different functional domains, an N-terminal domain important for membrane association, a central steroid binding site, and a C-terminal part mediating TeiR function. Finally, we could demonstrate that TeiR works as a kinase in the steroid signaling chain in C. testosteroni. Overall, we provide evidence that TeiR mediates steroid sensing and metabolism in C. testosteroni via its steroid binding and kinase activity.

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“…To elucidate the pathogenesis of APEC, we adapted signature-tagged transposon mutagenesis to a 5-week-old chicken model and identified 28 virulence-associated genes (Li et al, 2005). Among them, yjjQ encodes a putative transcriptional regulator since sequence analysis revealed that it harbours a helix-turn-helix (HTH) DNA-binding domain shared by all members of the LuxR family regulators (Chirwa & Herrington, 2003;Crater & Moran, 2001;Pruneda-Paz et al, 2004). The presence of yjjQ has been reported for commensal and various pathogenic bacteria such as enterohaemorrhagic E. coli (EHEC), uropathogenic E. coli (UPEC), Shigella and Salmonella by genomic sequencing.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a yjjQ mutant of avian pathogenic Escherichia coli (APEC)

Ewers

Laturnus

et al. 2008

Microbiology

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Infections with extraintestinal avian pathogenic Escherichia coli (APEC) cause significant economic losses in the poultry industry worldwide. In a previous study we applied signature-tagged transposon mutagenesis and identified 28 virulence-associated genes in APEC strain IMT5155 (O2 : H5 : K1). One of them, yjjQ, encodes a putative transcriptional regulator whose function and role in pathogenesis are still unknown. In the present study, this mutant has been characterized. The yjjQ-defective mutant of IMT5155 (M18E10) was out-competed by the wild-type strain in vivo, and infection of chickens with this yjjQ mutant led to strongly reduced bacterial loads in several organs. Expression studies showed that transcription of yjjQ was significantly upregulated in M9 minimal medium. Correspondingly, the yjjQ mutant showed significantly reduced growth in M9 medium. Although the mutation could not be complemented, a yjjQ deletion mutant showed phenotypes similar to the transposon-generated mutant M18E10, whereas deletion and overexpression of the downstream gene bglJ did not cause a growth defect in M9. To identify virulence genes regulated by YjjQ, one-and two-dimensional protein gel electrophoresis was performed. The proteomic analysis revealed that in the yjjQ mutant M18E10 the expression of several genes involved in iron uptake was downregulated and some other genes were upregulated. The regulation of genes involved in iron uptake was shown to occur at the transcription level using real-time RT-PCR. Taking the results together, this functional analysis strongly suggests that YjjQ is a regulator involved in virulence of APEC by affecting iron uptake.

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TeiR, a LuxR-Type Transcription Factor Required for Testosterone Degradation inComamonas testosteroni

Cited by 40 publications

References 42 publications

Steroid degradation in Comamonas testosteroni

Steroid degradation in Comamonas testosteroni

Testosterone-inducible Regulator Is a Kinase That Drives Steroid Sensing and Metabolism in Comamonas testosteroni

Characterization of a yjjQ mutant of avian pathogenic Escherichia coli (APEC)

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