ArticleThe protein journal2013
Heterologous expression and metal-binding characterization of a type 1 metallothionein isoform (OsMTI-1b) from rice (Oryza sativa).
Article in The protein journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 36 citations in OpenAlex.
- From copper homeostasis to cuproptosis: a new perspective on CNS immune regulation and neurodegenerative diseases.Frontiers in neurology · 2025Review
- Involvement of the Metallothionein gene OsMT2b in Drought and Cadmium Ions Stress in Rice.Rice (New York, N.Y.) · 2024Article
- Expression of the rgMT gene, encoding for a rice metallothionein-like protein in Saccharomyces cerevisiae and Arabidopsis thaliana.Journal of genetics · 2014Article
- Differential responses of three sweetpotato metallothionein genes to abiotic stress and heavy metals.Molecular biology reports · 2014Article
- Abiotic stress response in yeast and metal-binding ability of a type 2 metallothionein-like protein (PutMT2) from Puccinellia tenuiflora.Molecular biology reports · 2014Article
- Dehydroascorbate reductase and monodehydroascorbate reductase activities of two metallothionein-like proteins from sweet potato (Ipomoea batatas [L.] Lam. 'Tainong 57') storage roots.Botanical studies · 2013Article
- Heterologous expression of a rice metallothionein isoform (OsMTI-1b) in Saccharomyces cerevisiae enhances cadmium, hydrogen peroxide and ethanol tolerance.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metallothioneins (MTs) are ubiquitous, low molecular mass and cysteine-rich proteins that play important roles in maintaining intracellular metal homeostasis, eliminating metal toxification and protecting the cells against oxidative damages. MTs are able to bind metal ions through the thiol groups of their cysteine residues. Plants have several MT isoforms which are classified into four types based on the arrangement of cysteine residues. In the present study, a rice (Oryza sativa) gene encoding type 1 MT isoform, OsMTI-1b, was inserted in vector pET41a and overexpressed in Escherichia coli as carboxy-terminal extensions of glutathione-S-transferase (GST). The recombinant protein GST-OsMTI-1b was purified using affinity chromatography and its ability to bind with Ni(2+), Cd(2+), Zn(2+) and Cu(2+) ions was analyzed. The results demonstrated that this isoform has ability to bind Ni(2+), Cd(2+) and Zn(2+) ions in vitro, whereas it has no substantial ability to bind Cu(2+) ions. From competitive reaction with 5,5'-dithiobis(2-nitrobenzoic acid), DTNB, the affinity of metal ions for recombinant form of GST-OsMTI-1b was as follows: Ni(2+)/Cd(2+) > Zn(2+) > Cu(2+).
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