Binding of steroids by a partially purified periplasmic protein from Pseudomonas testosteroni

Watanabe, Mamoru; Sy, Luisa Po; Hunt, David; Lefebvre, Yvonne A.

doi:10.1016/0022-4731(79)90237-1

Cited by 9 publications

(2 citation statements)

References 14 publications

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“…The nodulation process is initiated by the secretion from the plant of a flavonoid, which stimulates the transcription of nodulation (nod) genes in the target rhizobia. The remarkable similarities between the actions of flavonoids in the communication between plants and rhizobia to that of steroidmediated actions in vertebrates (39), together with the occurrence of steroid-binding proteins and HSDs in bacteria (40,41), are relevant to the question whether the elements for transcriptional activation or inactivation of genes by steroid-like molecules are also present in procaryotes.…”

Section: Figmentioning

confidence: 99%

Regulation of the Steroid-inducible 3α-Hydroxysteroid Dehydrogenase/Carbonyl Reductase Gene in Comamonas testosteroni

Guan

Maser

2001

Journal of Biological Chemistry

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The Comamonas testosteroni 3␣-hydroxysteroid dehydrogenase/carbonyl reductase gene (hsdA) codes for an adaptive enzyme in the degradation of steroid compounds. However, no information was available on the molecular regulation of steroid-inducible genes nor on the mechanism of steroid signaling in procaryotes. We, therefore, investigated the cis-and trans-acting elements of hsdA expression to infer the mechanism of its molecular regulation by steroids. The gene was localized on a 5.257-kilobase EcoRI fragment of C. testosteroni chromosomal DNA. The promoter was characterized, and the transcriptional start site was identified. Two palindromic operator domains were found upstream of hsdA. A new gene coding for a trans-acting negative regulator (repressor A, RepA) of hsdA expression was characterized. The specific interaction between RepA, testosterone, and the operator domain is demonstrated. From our results we conclude that hsdA is under negative transcriptional control by an adjacent gene product (RepA). Accordingly, induction of hsdA by steroids in fact is a derepression, where steroidal inducers bind to the repressor, thereby preventing its binding to the hsdA operator.

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Section: Figmentioning

confidence: 99%

Regulation of the Steroid-inducible 3α-Hydroxysteroid Dehydrogenase/Carbonyl Reductase Gene in Comamonas testosteroni

Guan

Maser

2001

Journal of Biological Chemistry

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“…The involvement of a membrane-bound 3~ and 17~-hydroxysteriod dehydrogenase for testosterone transport was further suggested by experiments with inhibitors and antibodies for this dehydrogenase . Watanabe and his colleagues (Francis and Watanabe, 1981Watanabe et al, 1979) identified several binding proteins for steroids in the shock fluid and also in the membrane fraction of testosterone-grown P. testosteroni and partially purified the binding proteins. No evidence is obtained, however, that shows involvement of these binding proteins in the transport process of steroids in P. testosteroni.…”

Section: Steroidsmentioning

confidence: 99%

Pseudomonas

1998

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Localization of the steroid 1‐dehydrogenase in Rhodococcus erythropolis IMET 7030 by immunoelectron microscopy

Wagner¹,

Atrat²,

Clark‐Curtiss

et al. 1992

J. Basic Microbiol.

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The steroid 1-dehydrogenase of Rhodococcus erythropolis IMET 7030, an active steroid-transforming strain, was localized by immunogold labelling both in cells induced with 17-alpha-methyl-testosterone and in noninduced cells. The labelling intensity was much higher in induced cells than in noninduced cells, indicating increased enzyme production in the case of induction. Using the postembedding procedure, the main portion of the enzyme was found in the peripheral region of the cytoplasm. A considerable amount was bound in clusters to the inner side of the cytoplasmic membrane. The enzyme was also detected in channels connecting the cytoplasm with the cell surface. By means of the preembedding labelling, a few gold clusters could be detected on the cell surface. The significance of this observation was discussed.

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Binding of steroids by a partially purified periplasmic protein from Pseudomonas testosteroni

Cited by 9 publications

References 14 publications

Regulation of the Steroid-inducible 3α-Hydroxysteroid Dehydrogenase/Carbonyl Reductase Gene in Comamonas testosteroni

Regulation of the Steroid-inducible 3α-Hydroxysteroid Dehydrogenase/Carbonyl Reductase Gene in Comamonas testosteroni

Pseudomonas

Localization of the steroid 1‐dehydrogenase in Rhodococcus erythropolis IMET 7030 by immunoelectron microscopy

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