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Independent metal-thiolate cluster formation in C-terminal Cys-rich region of a rice type 1 metallothionein isoform.
Int J Biol Macromol. 2017 Mar; 96:436-441.IJ

Abstract

In this study we examined the independent self assembly of metal-binding in C-terminal Cys- rich region of a type 1 metallothionein (MT) isoform from rice (OsMTI-1b). To this end the N-terminal of OsMTI-1b (C-OsMTI-1b) was heterologously expressed in Escherichia coli as fusion protein with glutathione-S-transferase (GST). As compared with control (The E. coli cells containing pET41a without gene), transgenic E. coli cells expressing GST-C-OsMTI-1b accumulated more Ni2+, Cd2+, and Zn2+ from culture medium and showed increased tolerance against these metals. The recombinant GST-C-OsMTI-1b was purified using affinity chromatography. According to in vitro assays the protein GST-C-OsMTI-1b was able to form complexes with Ni2+, Cd2+ and Zn2+. These results demonstrate the formation of independent metal-thiolate cluster at C-terminal Cys-rich region of OsMTI-1b without participation of N-terminal Cys-rich region.

Authors+Show Affiliations

Department of Biotechnology, College of Agriculture, Isfahan University of Technology, Isfahan 84156-83111, Iran.Department of Biotechnology, College of Agriculture, Isfahan University of Technology, Isfahan 84156-83111, Iran. Electronic address: a.shahpiri@cc.iut.ac.ir.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

28013008

Citation

Malekzadeh, Rahim, and Azar Shahpiri. "Independent Metal-thiolate Cluster Formation in C-terminal Cys-rich Region of a Rice Type 1 Metallothionein Isoform." International Journal of Biological Macromolecules, vol. 96, 2017, pp. 436-441.
Malekzadeh R, Shahpiri A. Independent metal-thiolate cluster formation in C-terminal Cys-rich region of a rice type 1 metallothionein isoform. Int J Biol Macromol. 2017;96:436-441.
Malekzadeh, R., & Shahpiri, A. (2017). Independent metal-thiolate cluster formation in C-terminal Cys-rich region of a rice type 1 metallothionein isoform. International Journal of Biological Macromolecules, 96, 436-441. https://doi.org/10.1016/j.ijbiomac.2016.12.047
Malekzadeh R, Shahpiri A. Independent Metal-thiolate Cluster Formation in C-terminal Cys-rich Region of a Rice Type 1 Metallothionein Isoform. Int J Biol Macromol. 2017;96:436-441. PubMed PMID: 28013008.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Independent metal-thiolate cluster formation in C-terminal Cys-rich region of a rice type 1 metallothionein isoform. AU - Malekzadeh,Rahim, AU - Shahpiri,Azar, Y1 - 2016/12/21/ PY - 2016/07/30/received PY - 2016/12/14/revised PY - 2016/12/16/accepted PY - 2016/12/26/pubmed PY - 2017/4/26/medline PY - 2016/12/26/entrez KW - C-terminal Cys-rich region KW - Metal-thiolate cluster KW - Metallothionein KW - OsMTI-1b KW - Rice SP - 436 EP - 441 JF - International journal of biological macromolecules JO - Int J Biol Macromol VL - 96 N2 - In this study we examined the independent self assembly of metal-binding in C-terminal Cys- rich region of a type 1 metallothionein (MT) isoform from rice (OsMTI-1b). To this end the N-terminal of OsMTI-1b (C-OsMTI-1b) was heterologously expressed in Escherichia coli as fusion protein with glutathione-S-transferase (GST). As compared with control (The E. coli cells containing pET41a without gene), transgenic E. coli cells expressing GST-C-OsMTI-1b accumulated more Ni2+, Cd2+, and Zn2+ from culture medium and showed increased tolerance against these metals. The recombinant GST-C-OsMTI-1b was purified using affinity chromatography. According to in vitro assays the protein GST-C-OsMTI-1b was able to form complexes with Ni2+, Cd2+ and Zn2+. These results demonstrate the formation of independent metal-thiolate cluster at C-terminal Cys-rich region of OsMTI-1b without participation of N-terminal Cys-rich region. SN - 1879-0003 UR - https://www.unboundmedicine.com/medline/citation/28013008/Independent_metal_thiolate_cluster_formation_in_C_terminal_Cys_rich_region_of_a_rice_type_1_metallothionein_isoform_ DB - PRIME DP - Unbound Medicine ER -