ArticleJournal of bacteriology2004
Regulation of tetralin biodegradation and identification of genes essential for expression of thn operons.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 31 citations in OpenAlex.
- Revealing the essential role of the lid in mclPHA intracellular depolymerase from Pseudomonas putida KT2440.Applied microbiology and biotechnology · 2025Article
- Genetic Characterization of the Ibuprofen-Degradative Pathway of Rhizorhabdus wittichii MPO218.Applied and environmental microbiology · 2022Article
- An arsRB resistance operon confers tolerance to arsenite in the environmental isolate Terribacillus sp. AE2B 122.FEMS microbiology ecology · 2021Article
- Modulating redox metabolism to improve isobutanol production in Shimwellia blattae.Biotechnology for biofuels · 2021Article
- Identification of two fnr genes and characterisation of their role in the anaerobic switch in Sphingopyxis granuli strain TFA.Scientific reports · 2020Article
- Understanding the metabolism of the tetralin degrader Sphingopyxis granuli strain TFA through genome-scale metabolic modelling.Scientific reports · 2020Article
- Two paralogous EcfG σ factors hierarchically orchestrate the activation of the General Stress Response in Sphingopyxis granuli TFA.Scientific reports · 2020Article
- Review
- Sox transcription in sarcosine utilization is controlled by Sigma(54) and SoxR in Bacillus thuringiensis HD73.Scientific reports · 2016Article
- Genetic dissection of independent and cooperative transcriptional activation by the LysR-type activator ThnR at close divergent promoters.Scientific reports · 2016Article
- Engineering alternative isobutanol production platforms.AMB Express · 2015Article
- Fe-S proteins that regulate gene expression.Biochimica et biophysica acta · 2015Review
- Article
- ThnY is a ferredoxin reductase-like iron-sulfur flavoprotein that has evolved to function as a regulator of tetralin biodegradation gene expression.The Journal of biological chemistry · 2011Article
- Tetralin-induced and ThnR-regulated aldehyde dehydrogenase and beta-oxidation genes in Sphingomonas macrogolitabida strain TFA.Applied and environmental microbiology · 2010Article
- Molecular and biochemical characterization of the tetralin degradation pathway in Rhodococcus sp. strain TFB.Microbial biotechnology · 2009Article
- Integrated response to inducers by communication between a catabolic pathway and its regulatory system.Journal of bacteriology · 2007Article
- Oxygen-dependent regulation of the central pathway for the anaerobic catabolism of aromatic compounds in Azoarcus sp. strain CIB.Journal of bacteriology · 2006Article
- A new generation of vectors with increased induction ratios by overimposing a second regulatory level by attenuation.Nucleic acids research · 2005Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tetralin biodegradation genes of Sphingomonas macrogolitabida strain TFA are clustered in two closely linked and divergent operons. To analyze expression of both operons under different growth conditions, transcriptional and translational gene fusions of the first genes of each operon to lacZ have been constructed in plasmids unable to replicate in Sphingomonas and integrated by recombination into the genome of strain TFA. Expression analysis indicated that the transcription of both genes is induced in similar ways by the presence of tetralin. Gene expression in both operons is also subjected to overimposed catabolic repression. Two additional genes named thnR and thnY have been identified downstream of thnCA3A4 genes. ThnR is similar to LysR-type regulators, and mutational analysis indicated that ThnR is strictly required for expression of the thn operons. Unlike other LysR-type regulators, ThnR does not repress its own synthesis. In fact, ThnR activates its own expression, since thnR is cotranscribed with the thnCA3A4 genes. ThnY is similar to the ferredoxin reductase components of dioxygenase systems and shows the fer2 domain, binding a Cys4[2Fe-2S] iron sulfur center, and the FAD-binding domain, common to those reductases. However, it lacks the NAD-binding domain. Intriguingly, ThnY has a regulatory role, since it is also strictly required for expression of the thn operons. Given the similarity of ThnY to reductases and the possibility of its being present in the two redox states, it is tempting to speculate that ThnY is a regulatory component connecting expression of the thn operons to the physiological status of the cell.
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