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Delineation of the functional and structural properties of the glutathione transferase family from the plant pathogen Erwinia carotovora

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Abstract

Erwinia carotovora, a widespread plant pathogen that causes soft rot disease in many plants, is considered a major threat in agriculture. Bacterial glutathione transferases (GSTs) play important roles in a variety of metabolic pathways and processes, such as the biodegradation of xenobiotics, protection against abiotic stress, and resistance against antimicrobial drugs. The GST family of canonical soluble enzymes from Erwinia carotovora subsp. atroseptica strain SCRI1043 (EcaGSTs) was investigated. Genome analysis showed the presence of six putative canonical cytoplasmic EcaGSTs, which were revealed by phylogenetic analysis to belong to the well-characterized GST classes beta, nu, phi, and zeta. The analysis also revealed the presence of two isoenzymes that were phylogenetically close to the omega class of GSTs, but formed a distinct class. The EcaGSTs were cloned and expressed in Escherichia coli, and their catalytic activity toward different electrophilic substrates was elucidated. The EcaGSTs catalyzed different types of reactions, although all enzymes were particularly active in reactions involving electrophile substitution. Gene and protein expression profiling conducted under normal culture conditions as well as in the presence of the herbicide alachlor and the xenobiotic 1-chloro-2,4-dinitrobenzene (CDNB) showed that the isoenzyme EcaGST1, belonging to the omega-like class, was specifically induced at both the protein and mRNA levels. EcaGST1 presumably participates in counteracting the xenobiotic toxicity and/or abiotic stress conditions, and may therefore represent a novel molecular target in the development of new chemical treatments to control soft rot diseases.

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Funding

This research work received funding from the International Scientific Partnership Program at King Saud University, Saudi Arabia, through ISPP# 0071.

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Authors and Affiliations

  1. Laboratory of Enzyme Technology, Department of Biotechnology, School of Food, Biotechnology and Development, Agricultural University of Athens, 75 Iera Odos Street, 118 55, Athens, Greece

    Christina Theoharaki, Evangelia Chronopoulou, Panagiotis Giannopoulos, Sofia Maurikou, Katholiki Skopelitou & Nikolaos E. Labrou

  2. Laboratory of Genetics, Department of Biotechnology, School of Food, Biotechnology and Development, Agricultural University of Athens, 75 Iera Odos Street, 118 55, Athens, Greece

    Dimitrios Vlachakis

  3. Department of Biochemistry, College of Science, King Saud University, P.O. Box 2455, Riyadh, 11451, Saudi Arabia

    Farid S. Ataya

  4. Molecular Biology Department, Genetic Engineering Division, National Research Centre, 33 El-Bohouth St., Dokki, Giza, P.O. 12622, Egypt

    Farid S. Ataya

  5. Turku Centre for Biotechnology, University of Turku and Åbo Akademi University, FI-20521, Turku, Finland

    Anastassios C. Papageorgiou

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  1. Christina Theoharaki
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  2. Evangelia Chronopoulou
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  8. Anastassios C. Papageorgiou
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  9. Nikolaos E. Labrou
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Correspondence to Nikolaos E. Labrou.

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Theoharaki, C., Chronopoulou, E., Vlachakis, D. et al. Delineation of the functional and structural properties of the glutathione transferase family from the plant pathogen Erwinia carotovora. Funct Integr Genomics 19, 1–12 (2019). https://doi.org/10.1007/s10142-018-0618-8

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