کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8332097 | 1540247 | 2015 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Functional characterization of a type 3 metallolthionein isoform (OsMTI-3a) from rice
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کلمات کلیدی
IPTGphytochelatinsGSTOryza sativaDTNBMRETNB2-nitro-5-thiobenzoic acid - 2-نیترو -5-تیوبنزوئیک اسیدisopropyl β-D-1-thiogalactopyranoside - ایزوپروپیل β-D-1-thiogalactopyranosideRice - برنجHeterologous expression - بیان هترولوژیکMetal-responsive element - عنصر پاسخگو فلزHeavy metals - فلزات سنگینLuria-Bertani - لواریا بارتانیMetallothionein - متالوتونیئینFunctional characterization - ویژگی های عملکردیglutathione-S-transferase - گلوتاتیون S-ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Functional characterization of a type 3 metallolthionein isoform (OsMTI-3a) from rice Functional characterization of a type 3 metallolthionein isoform (OsMTI-3a) from rice](/preview/png/8332097.png)
چکیده انگلیسی
Metallothioneins (MTs) are low-molecular weight proteins with high Cys content and a high affinity for metals. Plant MTs are classified into four types based on the arrangement of Cys in their amino acid sequences. In the present study, the gene encoding OsMTI-3a, a type 3 MT found in rice, was cloned into pET41a vector. The resulting construct was transformed into the Escherichia coli strain Rosetta (DE3). Following the induction with isopropyl β-d-1-thiogalactopyranoside, the OsMTI-3a was expressed as glutathione-S-transferase (GST)-tagged fusion protein. In comparison to control strain, the cells expressing GST-OsMTI-3a accumulated more Cd2+, Ni2+ and Zn2+ when they were grown in the medium containing CdCl2, NiCl2 or ZnSO4. The recombinant GST-OsMTI-3a was purified using affinity chromatography. The UV absorption spectra recorded after the reconstitution of the apo-protein with different metals confirmed that GST-OsMTI-3a was able to form complexes with Cd2+, Ni2+, and Zn2+. The reaction of the protein-metal complexes with 5-5-dithiobis (2-nitrobenzoic) revealed that the order of affinity of GST-OsMTI-3a toward different metals was Ni2+ â¥Â Cd2+ > Zn2+ > Cu2+.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 73, February 2015, Pages 154-159
Journal: International Journal of Biological Macromolecules - Volume 73, February 2015, Pages 154-159
نویسندگان
Azar Shahpiri, Iman Soleimanifard, Mohammad Ali Asadollahi,