Cloning and characterization of styrene catabolism genes from Pseudomonas fluorescens ST

Article Abstract:

The genes from Pseudomonas fluorescens ST, responsible for the initial steps of styrene degradation, are arranged in a cluster and appear to be encoded by the same DNA strand. Cloning of the genes reveals the presence of monooxygenase, epoxystyrene isomerase, and epoxystyrene reductase activities. The monooxygenase and epoxystyrene isomerase genes are present on the same DNA strand and their expression depends on the pTZ19 lacZp activity. The activity of the epoxystyrene reductase gene depends on an internal promoter.

author: Ruzzi, Maurizio, Beltrametti, Fabrizio, Galli, Enrica, Zennaro, Elisabetta, Marconi, Andrea M., Bestetti, Giuseppina, Solinas, Francesca
Observations, Amino acid sequence, Amino acid sequencing

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Dual role of response regulator StyR in styrene catabolism regulation

Article Abstract:

StyR is able to bind PstyA at three distinct sites with different affinities and that, depending on which site is occupies, this regulator can act as an activator or as a repressor and play a major role in carbon catabolite repression control. Moreover, it is found that the upstream StyR site and the integration host factor (IHF) binding site overlap, suggesting that the interaction of the StyR and IHF could play a role in the fine modulation of expression of the styrene catabolic gene.

author: Leoni, Livia, Rampioni, Giordano, Stefano, Valeria Di, Zennaro, Elisabetta
Science & research, Pseudomonas, Styrene, Chemical properties, Catabolism

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Sequencing and functional analysis of styrene catabolism genes from Pseudomonas fluorescens ST

Article Abstract:

The nucleotide sequence of the 4,377-bp chromosomal region of Pseudomonas fluorescens ST that codes for the oxidation of styrene to phenylacetic acid was identified. StyA was observed to be weakly homologous to p-hydroxybenzoate hydroxylase from both P. fluorescens and P. aeruginosa and to salicylate hydroxylase from P. putida. This indicated that it might be a flavin adenine dinucleotide-binding monooxygenase.

author: Ruzzi, Maurizio, Galli, Enrica, Zennaro, Elisabetta, Marconi, Andrea M., Bestetti, Giuseppina, Beltrametti, Frabrizio, Colombo, Cristiano
Genetic aspects

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subjects list: Research, Microbial metabolism, Pseudomonas fluorescens
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