Tags

Type your tag names separated by a space and hit enter

N-Terminal Cys-Rich Region of a Rice Type 1 Metallothionein Independently Forms Metal-Thiolate Cluster.
Protein Pept Lett. 2016; 23(7):639-44.PP

Abstract

The members of plant metallothionein (MT) subfamily p1 are characterized with the presence of six Cys at each end of N- and C-terminal of their amino acid sequences which are arranged in a CXCXXXCXCXXXCXC and CXCXXXCXCXXCXC sequence, respectively. In this study we evaluated the independence of N-terminal Cys-rich region of a type 1 MT isoform from rice (OsMTI- 1b) in forming metal-thiolate cluster. To this end the N-terminal of OsMTI-1b (N-OsMTI-1b) was heterologously expressed in Escherichia coli as fusion protein with glutathione-S-transferase (GST). The E.coli cells expressing GST-N-OsMTI-1b were able to remove Cd2+ and Ni2+ from culture medium. The recombinant GST-N-OsMTI-1b was purified using affinity chromatography. The UV absorption spectra recorded after the reconstitution of the apo-protein with Cd2+ and Ni2+ confirmed that GST-N-OsMTI-1b was able to form complexes with Cd2+ and Ni2+. These results demonstrate the formation of independent metal-thiolate cluster at Nterminal Cys-rich region of GST-N-OsMTI-1b without participation of C-terminal Cys-rich region.

Authors+Show Affiliations

No affiliation info availableDepartment of Biotechnology, College of Agriculture, Isfahan University of Technology, Isfahan 84156- 83111, Iran. a.shahpiri@cc.iut.ac.ir.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

27165409

Citation

Ahmadi, Soheila, and Azar Shahpiri. "N-Terminal Cys-Rich Region of a Rice Type 1 Metallothionein Independently Forms Metal-Thiolate Cluster." Protein and Peptide Letters, vol. 23, no. 7, 2016, pp. 639-44.
Ahmadi S, Shahpiri A. N-Terminal Cys-Rich Region of a Rice Type 1 Metallothionein Independently Forms Metal-Thiolate Cluster. Protein Pept Lett. 2016;23(7):639-44.
Ahmadi, S., & Shahpiri, A. (2016). N-Terminal Cys-Rich Region of a Rice Type 1 Metallothionein Independently Forms Metal-Thiolate Cluster. Protein and Peptide Letters, 23(7), 639-44.
Ahmadi S, Shahpiri A. N-Terminal Cys-Rich Region of a Rice Type 1 Metallothionein Independently Forms Metal-Thiolate Cluster. Protein Pept Lett. 2016;23(7):639-44. PubMed PMID: 27165409.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - N-Terminal Cys-Rich Region of a Rice Type 1 Metallothionein Independently Forms Metal-Thiolate Cluster. AU - Ahmadi,Soheila, AU - Shahpiri,Azar, PY - 2015/10/19/received PY - 2016/05/06/revised PY - 2016/05/07/accepted PY - 2016/5/12/entrez PY - 2016/5/12/pubmed PY - 2017/3/21/medline SP - 639 EP - 44 JF - Protein and peptide letters JO - Protein Pept Lett VL - 23 IS - 7 N2 - The members of plant metallothionein (MT) subfamily p1 are characterized with the presence of six Cys at each end of N- and C-terminal of their amino acid sequences which are arranged in a CXCXXXCXCXXXCXC and CXCXXXCXCXXCXC sequence, respectively. In this study we evaluated the independence of N-terminal Cys-rich region of a type 1 MT isoform from rice (OsMTI- 1b) in forming metal-thiolate cluster. To this end the N-terminal of OsMTI-1b (N-OsMTI-1b) was heterologously expressed in Escherichia coli as fusion protein with glutathione-S-transferase (GST). The E.coli cells expressing GST-N-OsMTI-1b were able to remove Cd2+ and Ni2+ from culture medium. The recombinant GST-N-OsMTI-1b was purified using affinity chromatography. The UV absorption spectra recorded after the reconstitution of the apo-protein with Cd2+ and Ni2+ confirmed that GST-N-OsMTI-1b was able to form complexes with Cd2+ and Ni2+. These results demonstrate the formation of independent metal-thiolate cluster at Nterminal Cys-rich region of GST-N-OsMTI-1b without participation of C-terminal Cys-rich region. SN - 1875-5305 UR - https://www.unboundmedicine.com/medline/citation/27165409/N_Terminal_Cys_Rich_Region_of_a_Rice_Type_1_Metallothionein_Independently_Forms_Metal_Thiolate_Cluster_ DB - PRIME DP - Unbound Medicine ER -