Independent metal-thiolate cluster formation in C-terminal Cys-rich region of a rice type 1 metallothionein isoform.
Identifieur interne : 000089 ( Main/Exploration ); précédent : 000088; suivant : 000090Independent metal-thiolate cluster formation in C-terminal Cys-rich region of a rice type 1 metallothionein isoform.
Auteurs : Rahim Malekzadeh [Iran] ; Azar Shahpiri [Iran]Source :
- International journal of biological macromolecules [ 1879-0003 ] ; 2017.
Descripteurs français
- KwdFr :
- Clonage moléculaire (MeSH), Composés organométalliques (composition chimique), Cystéine (MeSH), Mutation (MeSH), Métallothionéine (composition chimique), Métallothionéine (génétique), Oryza (MeSH), Protéines végétales (composition chimique), Stabilité protéique (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Composés organométalliques, Métallothionéine, Protéines végétales.
- génétique : Métallothionéine.
- Clonage moléculaire, Cystéine, Mutation, Oryza, Stabilité protéique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Metallothionein, Organometallic Compounds, Plant Proteins.
- chemical , genetics : Metallothionein.
- chemical : Cysteine.
- Amino Acid Sequence, Cloning, Molecular, Mutation, Oryza, Protein Stability.
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.
DOI: 10.1016/j.ijbiomac.2016.12.047
PubMed: 28013008
Affiliations:
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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 Ni<sup>2+</sup>, Cd<sup>2+</sup>, and Zn<sup>2+</sup> 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 Ni<sup>2+</sup>, Cd<sup>2+</sup> and Zn<sup>2+</sup>. 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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28013008</PMID><DateCompleted><Year>2017</Year><Month>04</Month><Day>25</Day></DateCompleted><DateRevised><Year>2018</Year><Month>05</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0003</ISSN><JournalIssue CitedMedium="Internet"><Volume>96</Volume><PubDate><Year>2017</Year><Month>Mar</Month></PubDate></JournalIssue><Title>International journal of biological macromolecules</Title><ISOAbbreviation>Int J Biol Macromol</ISOAbbreviation></Journal><ArticleTitle>Independent metal-thiolate cluster formation in C-terminal Cys-rich region of a rice type 1 metallothionein isoform.</ArticleTitle><Pagination><MedlinePgn>436-441</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0141-8130(16)31055-8</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ijbiomac.2016.12.047</ELocationID><Abstract><AbstractText>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 Ni<sup>2+</sup>, Cd<sup>2+</sup>, and Zn<sup>2+</sup> 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 Ni<sup>2+</sup>, Cd<sup>2+</sup> and Zn<sup>2+</sup>. 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.</AbstractText><CopyrightInformation>Copyright © 2016 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Malekzadeh</LastName><ForeName>Rahim</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, College of Agriculture, Isfahan University of Technology, Isfahan 84156-83111, Iran.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shahpiri</LastName><ForeName>Azar</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, College of Agriculture, Isfahan University of Technology, Isfahan 84156-83111, Iran. 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