Expression in<i>Escherichia coli</i>of Biphenyl 2,3-Dioxygenase Genes from a Gram-Positive Polychlorinated Biphenyl Degrader,<i>Rhodococcus jostii</i>RHA1

Ohmori, Tsuneo; Morita, Hirokazu; Tanaka, Megumi; Tomoi, Masanori; Miyauchi, Keisuke; Kasai, Daisuke; Furukawa, Koichi; Masai, Eiji; Fukuda, Masao

doi:10.1271/bbb.100452

Cited by 2 publications

(1 citation statement)

References 43 publications

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“…Since different subsets of bph genes have been successfully expressed in Escherichia coli (e.g., refs. 27 , 28 ), we designed a functional complementation scheme for this host. The coding sequence of SDR57C was thus placed under the control of a T7 promoter (p T7 ) in pGW-SDR ( Fig.…”

Section: Resultsmentioning

confidence: 99%

A poplar short-chain dehydrogenase reductase plays a potential key role in biphenyl detoxification

Contreras

Merino

Álvarez

et al. 2021

Proc. Natl. Acad. Sci. U.S.A.

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Polychlorinated biphenyls (PCBs) are persistent organic pollutants with severe effects on human health and the biosphere. Plant-based remediation offers many benefits over conventional PCB remediation, but its development has been hampered by our poor understanding of biphenyl metabolism in eukaryotes, among other factors. We report here a major PCB-responsive protein in poplar, a plant model system capable of PCB uptake and translocation. We provide structural and functional evidence that this uncharacterized protein, termed SDR57C, belongs to the heterogeneous short-chain dehydrogenase reductase (SDR) superfamily. Despite sequence divergence, structural modeling hinted at structural and functional similarities between SDR57C and BphB, a central component of the Bph pathway for biphenyl/PCB degradation in aerobic bacteria. By combining gas chromatography/mass spectrometry (GC/MS) profiling with a functional complementation scheme, we found that poplar SDR57C can replace BphB activity in the upper Bph pathway of Pseudomonas furukawaii KF707 and therefore catalyze the oxidation of 2,3-dihydro-2,3-dihydroxybiphenyl (2,3-DHDB) to 2,3-dihydroxybiphenyl (2,3-DHB). Consistent with this biochemical activity, we propose a mechanism of action based on prior quantum studies, general properties of SDR enzymes, and the modeled docking of 2,3-DHDB to the SDR57C-NAD+ complex. The putative detoxifying capacity of SDR57C was substantiated through reverse genetics in Arabidopsis thaliana. Phenotypic characterization of the SDR lines underscored an inducible plant pathway with the potential to catabolize toxic biphenyl derivatives. Partial similarities with aerobic bacterial degradation notwithstanding, real-time messenger RNA quantification indicates the occurrence of plant-specific enzymes and features. Our results may help explain differences in degradative abilities among plant genotypes and also provide elements to improve them.

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Section: Resultsmentioning

confidence: 99%

A poplar short-chain dehydrogenase reductase plays a potential key role in biphenyl detoxification

Contreras

Merino

Álvarez

et al. 2021

Proc. Natl. Acad. Sci. U.S.A.

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Degradation of Triclosan in the Water Environment by Microorganisms: A Review

Yin

Jiang³

et al. 2022

Microorganisms

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Triclosan (TCS), a kind of pharmaceuticals and personal care products (PPCPs), is widely used and has had a large production over years. It is an emerging pollutant in the water environment that has attracted global attention due to its toxic effects on organisms and aquatic ecosystems, and its concentrations in the water environment are expected to increase since the COVID-19 pandemic outbreak. Some researchers found that microbial degradation of TCS is an environmentally sustainable technique that results in the mineralization of large amounts of organic pollutants without toxic by-products. In this review, we focus on the fate of TCS in the water environment, the diversity of TCS-degrading microorganisms, biodegradation pathways and molecular mechanisms, in order to provide a reference for the efficient degradation of TCS and other PPCPs by microorganisms.

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Expression inEscherichia coliof Biphenyl 2,3-Dioxygenase Genes from a Gram-Positive Polychlorinated Biphenyl Degrader,Rhodococcus jostiiRHA1

Cited by 2 publications

References 43 publications

A poplar short-chain dehydrogenase reductase plays a potential key role in biphenyl detoxification

A poplar short-chain dehydrogenase reductase plays a potential key role in biphenyl detoxification

Degradation of Triclosan in the Water Environment by Microorganisms: A Review

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