Styrene is sensed by the N-terminal PAS sensor domain of StyS, a double sensor kinase from the styrene-degrading bacterium Pseudomonas fluorescens ST

Massai, Francesco; Rampioni, Giordano; Micolonghi, Chiara; Messina, Marco; Zennaro, Elisabetta; Ascenzi, Paolo; Leoni, Livia

doi:10.1007/s13213-014-0931-y

Cited by 4 publications

(4 citation statements)

References 16 publications

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“…As an example, in P. fluorescens ST, the StyR response regulator acts as an activator of the styrene catabolic operon when intermediate phosphorylation levels drive its binding to high-affinity sites on the P styA promoter. When its phosphorylation level increases, StyR turns into a repressor of the styrene catabolic operon by binding to a low-affinity binding site on P styA ( 78 – 80 ). Dual-function transcriptional regulators have been described also among QS regulators.…”

Section: Discussionmentioning

confidence: 99%

PqsE Expands and Differentially Modulates the RhlR Quorum Sensing Regulon in Pseudomonas aeruginosa

et al. 2022

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The ability of Pseudomonas aeruginosa to cause difficult-to-treat infections relies on its capacity to fine-tune the expression of multiple virulence traits via the las , rhl , and pqs QS systems. Both the pqs effector protein PqsE and the rhl transcriptional regulator RhlR are required for full production of key virulence factors in vitro and pathogenicity in vivo .

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Section: Discussionmentioning

confidence: 99%

PqsE Expands and Differentially Modulates the RhlR Quorum Sensing Regulon in Pseudomonas aeruginosa

et al. 2022

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“…In this context, we propose that LasR exerts a direct repression by its binding to phzA1 Las-box and an indirect negative effect on phzA1 expression, through its activation of rsaL expression. The exact mechanism of this direct negative regulation exerted by LasR remains to be elucidated, there are reports of transcriptional regulators that can switch between positive/negative regulation depending on phosphorylation levels, as seen in Pseudomonas fluorescens [41], or on sequence positioning of the binding sites, as seen in Vibrio alginolyticus [42], even in P. aeruginosa , the RhlR QS regulator has been suggested to act in both ways [35, 43], the case of LasR could be a similar situation to be determinate.…”

Section: Discussionmentioning

confidence: 99%

Pseudomonas aeruginosa LasR overexpression leads to a RsaL-independent pyocyanin production inhibition in a low phosphate condition

et al. 2022

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Several Pseudomonas aeruginosa virulence-related traits like pyocyanin are regulated by an intricate regulatory network called quorum sensing (QS) that relies on transcriptional regulators that are activated through binding to a self-produced molecule called an autoinducer (AI). QS is composed of three systems, Las, Rhl and Pqs. In the Las system, the regulatory protein LasR interacts with its AI to activate the other two QS systems. In turn, the Rhl and Pqs systems regulate the expression of multiple virulence-related genes, such as the genes of the reiterated operons phzA1B1C1D1E1F1G1 and phzA2B2C2D2E2F2G2 involved in pyocyanin production. The Las system also regulates the negative regulator RsaL, which provides negative feedback to the QS-response, including repression of pyocyanin synthesis genes. In this work, we describe that LasR can act as a negative regulator of phzA1 transcription and hence of pyocyanin production and that this regulation is independent of RsaL activity. This work contributes to the understanding of QS-dependent pyocyanin production and demonstrates a previously uncharacterized role of LasR as a repressor.

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“…11 The presence of styrene in cytoplasm activates the two-component regulatory system of styrene operon called "styS/styR," via phosphorylation. 21,22 The activated StyS/R binds to the promoter region of styA and initiates the transcription of styrene operon, resulting in the synthesis of styrene catabolic enzymes. 23 The styrene catabolism starts with the oxidation of the vinyl double bond to styrene oxide by SMO, a two-component flavozyme composed of highly conserved NADH-specific flavin reductase encoded by styB and flavin adenine dinucleotide (FAD)-specific styrene epoxidase encoded by styA that.…”

Section: Introductionmentioning

confidence: 99%

“…The styrene monomers enter the cytoplasm through a transmembrane protein located in the bacterial cell membrane called “StyE”; however, the presence and function of styE gene has only been validated in Pseudomonas putida CA‐3 11 . The presence of styrene in cytoplasm activates the two‐component regulatory system of styrene operon called “ styS/styR ,” via phosphorylation 21,22 . The activated StyS/R binds to the promoter region of styA and initiates the transcription of styrene operon, resulting in the synthesis of styrene catabolic enzymes 23 …”

Section: Introductionmentioning

confidence: 99%

Understanding the in silico aspects of bacterial catabolic cascade for styrene degradation

2022

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Styrene is a nonpolar organic compound used in very high volume for the industrial scale production of commercially important polymers such as polystyrene resins as well as copolymers like acrylonitrile butadiene styrene, latex, and rubber. These resins are widely used in the manufacturing of various products including single‐use plastics such as disposable cups and containers, protective packaging, heat insulation, and so forth. The large‐scale utilization leads to the over‐accumulation of styrene waste in the environment causing deleterious health risks including cancer, neurological impairment, dysbiosis of central nervous system, and respiratory problems. To eliminate the accumulating waste. Microbial enzyme‐based system represents the most environmental friendly and sustainable approach for elimination of styrene waste. However, comprehensive understanding of the enzyme–substrate interaction and associated pathways would be crucial for developing large‐scale disposal systems. This study aims to understand the molecular interaction between the protein‐ligand complexes of the styrene catabolic reactions by bacterial enzymes of sty operon. Molecular docking analysis for catalytic enzymes namely, styrene monooxygenase (SMO), styrene oxide isomerase (SOI), and phenylacetaldehyde dehydrogenase (PAD) of the bacterial sty operon was carried out with their individual substrates, that is, styrene, styrene oxide, and phenylacetic acid, respectively. The binding energy, amino acids forming binding cavity, and binding interactions between the protein‐ligand binding sites were calculated for each case. The obtained binding energies showed a stable association of these complexes indicating the future scope of their utilization for large‐scale bioremediation of styrene, and its commercially used polymers and copolymers.

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Styrene is sensed by the N-terminal PAS sensor domain of StyS, a double sensor kinase from the styrene-degrading bacterium Pseudomonas fluorescens ST

Cited by 4 publications

References 16 publications

PqsE Expands and Differentially Modulates the RhlR Quorum Sensing Regulon in Pseudomonas aeruginosa

PqsE Expands and Differentially Modulates the RhlR Quorum Sensing Regulon in Pseudomonas aeruginosa

Pseudomonas aeruginosa LasR overexpression leads to a RsaL-independent pyocyanin production inhibition in a low phosphate condition

Understanding the in silico aspects of bacterial catabolic cascade for styrene degradation

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