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.
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 -