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Bioaccumulation of Arsenic by Engineered Escherichia coli Cells Expressing Rice Metallothionein Isoforms.
Curr Microbiol. 2018 Nov; 75(11):1537-1542.CM

Abstract

Metallothioneins (MTs) are low-molecular weight cysteine (Cys)-rich proteins with high metal-binding capacity. Based on the Cys arrangement in their amino acid sequences, plant MTs are categorized into four classes. This study evaluated the ability of genetically engineered Escherichia coli cells, which express four rice MT isoforms as fusion proteins with glutathione-S-transferase (GST), to remove arsenic. As compared with control strain, the expression of GST-OsMT1, GST-OsMT2, GST-OsMT3, and GST-OsMT4 resulted in 8-, 5.6-, 3-, and 1.1-fold-higher As3+ accumulation. The recombinant GST-OsMT isoforms were purified using affinity chromatography and their apo-forms were prepared. The ability of the GST-OsMT2 isoform to bind with As3+ in vitro was also confirmed by ultraviolet (UV) absorption spectra recorded after the reconstitution of apo-proteins with As3+. However, the formation of complexes of other MT isoforms with arsenic was not observed.

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Publisher Full Text (DOI)

Authors+Show Affiliations

Shahpiri A
Department of Biotechnology, College of Agriculture, Isfahan University of Technology, 84156-83111, Isfahan, Iran. a.shahpiri@cc.iut.ac.ir.
Mohammadzadeh A
Department of Biotechnology, College of Agriculture, Isfahan University of Technology, 84156-83111, Isfahan, Iran.

MeSH

ArsenicEscherichia coliGenetic EngineeringMetallothioneinOryzaPlant ProteinsProtein IsoformsRecombinant Proteins

Pub Type(s)

Journal Article

Language

eng

PubMed ID

30151557

Citation

Shahpiri, Azar, and Asghar Mohammadzadeh. "Bioaccumulation of Arsenic By Engineered Escherichia Coli Cells Expressing Rice Metallothionein Isoforms." Current Microbiology, vol. 75, no. 11, 2018, pp. 1537-1542.
Shahpiri A, Mohammadzadeh A. Bioaccumulation of Arsenic by Engineered Escherichia coli Cells Expressing Rice Metallothionein Isoforms. Curr Microbiol. 2018;75(11):1537-1542.
Shahpiri, A., & Mohammadzadeh, A. (2018). Bioaccumulation of Arsenic by Engineered Escherichia coli Cells Expressing Rice Metallothionein Isoforms. Current Microbiology, 75(11), 1537-1542. https://doi.org/10.1007/s00284-018-1556-3
Shahpiri A, Mohammadzadeh A. Bioaccumulation of Arsenic By Engineered Escherichia Coli Cells Expressing Rice Metallothionein Isoforms. Curr Microbiol. 2018;75(11):1537-1542. PubMed PMID: 30151557.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Bioaccumulation of Arsenic by Engineered Escherichia coli Cells Expressing Rice Metallothionein Isoforms. AU - Shahpiri,Azar, AU - Mohammadzadeh,Asghar, Y1 - 2018/08/27/ PY - 2018/03/19/received PY - 2018/08/22/accepted PY - 2018/8/29/pubmed PY - 2018/11/9/medline PY - 2018/8/29/entrez SP - 1537 EP - 1542 JF - Current microbiology JO - Curr Microbiol VL - 75 IS - 11 N2 - Metallothioneins (MTs) are low-molecular weight cysteine (Cys)-rich proteins with high metal-binding capacity. Based on the Cys arrangement in their amino acid sequences, plant MTs are categorized into four classes. This study evaluated the ability of genetically engineered Escherichia coli cells, which express four rice MT isoforms as fusion proteins with glutathione-S-transferase (GST), to remove arsenic. As compared with control strain, the expression of GST-OsMT1, GST-OsMT2, GST-OsMT3, and GST-OsMT4 resulted in 8-, 5.6-, 3-, and 1.1-fold-higher As3+ accumulation. The recombinant GST-OsMT isoforms were purified using affinity chromatography and their apo-forms were prepared. The ability of the GST-OsMT2 isoform to bind with As3+ in vitro was also confirmed by ultraviolet (UV) absorption spectra recorded after the reconstitution of apo-proteins with As3+. However, the formation of complexes of other MT isoforms with arsenic was not observed. SN - 1432-0991 UR - https://www.unboundmedicine.com/medline/citation/30151557/Bioaccumulation_of_Arsenic_by_Engineered_Escherichia_coli_Cells_Expressing_Rice_Metallothionein_Isoforms_ DB - PRIME DP - Unbound Medicine ER -