Characterization analysis and heavy metal‐binding properties of CsMTL3 in Escherichia coli. Issue 11 (19th September 2018)
- Record Type:
- Journal Article
- Title:
- Characterization analysis and heavy metal‐binding properties of CsMTL3 in Escherichia coli. Issue 11 (19th September 2018)
- Main Title:
- Characterization analysis and heavy metal‐binding properties of CsMTL3 in Escherichia coli
- Authors:
- Xu, Xing
Duan, Ling
Yu, Jingwen
Su, Chenggang
Li, Jinhua
Chen, Dan
Zhang, Xingguo
Song, Hongyuan
Pan, Yu - Abstract:
- Abstract : Members of the metallothionein (MT) superfamily are involved in coordinating transition metal ions. In plants, MT family members are characterized by their arrangement of Cys residues. In this study, one member of the MT superfamily, CsMTL3, was characterized from a complementary DNA (cDNA) library from young cucumber fruit; CsMTL3 is predicted to encode a 64 amino acid protein with a predicted molecular mass of 6.751 kDa. Phylogenetic analysis identified it as a type 3 family member as the arrangement of N‐terminal Cys residues was different from that of MT‐like 2. Heterologous expression of CsMTL3 in Escherichia coli improved their heavy metal tolerance, particularly to Cd 2+ and Cu 2+, and led to increased uptake of Cd 2+ and Cu 2+ ; increased uptake was also observed for cells expressing Arabidopsis thaliana metallothionein 3 (AtMT3) and phytochelatin‐like (PCL), with greatest uptake in PCL‐expressing cells. These findings demonstrate that CsMTL3 can improve metal tolerance, especially for Cd 2+ ions, when heterologously expressed in E. coli, and suggest that the composition and arrangement of N‐terminal Cys residues are associated with binding capacity and preference for different metal ions. Abstract : Metallothioneins (MTs) are among the most well‐characterized heavy metal‐binding ligands in plants. RT‐qPCR and heterologous expression analysis revealed that CsMTL3 significantly improves heavy metal tolerance, and enhances heavy metal uptake. Our resultsAbstract : Members of the metallothionein (MT) superfamily are involved in coordinating transition metal ions. In plants, MT family members are characterized by their arrangement of Cys residues. In this study, one member of the MT superfamily, CsMTL3, was characterized from a complementary DNA (cDNA) library from young cucumber fruit; CsMTL3 is predicted to encode a 64 amino acid protein with a predicted molecular mass of 6.751 kDa. Phylogenetic analysis identified it as a type 3 family member as the arrangement of N‐terminal Cys residues was different from that of MT‐like 2. Heterologous expression of CsMTL3 in Escherichia coli improved their heavy metal tolerance, particularly to Cd 2+ and Cu 2+, and led to increased uptake of Cd 2+ and Cu 2+ ; increased uptake was also observed for cells expressing Arabidopsis thaliana metallothionein 3 (AtMT3) and phytochelatin‐like (PCL), with greatest uptake in PCL‐expressing cells. These findings demonstrate that CsMTL3 can improve metal tolerance, especially for Cd 2+ ions, when heterologously expressed in E. coli, and suggest that the composition and arrangement of N‐terminal Cys residues are associated with binding capacity and preference for different metal ions. Abstract : Metallothioneins (MTs) are among the most well‐characterized heavy metal‐binding ligands in plants. RT‐qPCR and heterologous expression analysis revealed that CsMTL3 significantly improves heavy metal tolerance, and enhances heavy metal uptake. Our results demonstrate that CsMTL3 is a candidate gene for improving metal tolerance, and provide insights for future studies of the function of CsMTL3 in plants. … (more)
- Is Part Of:
- FEBS open bio. Volume 8:Issue 11(2018)
- Journal:
- FEBS open bio
- Issue:
- Volume 8:Issue 11(2018)
- Issue Display:
- Volume 8, Issue 11 (2018)
- Year:
- 2018
- Volume:
- 8
- Issue:
- 11
- Issue Sort Value:
- 2018-0008-0011-0000
- Page Start:
- 1820
- Page End:
- 1829
- Publication Date:
- 2018-09-19
- Subjects:
- CsMTL3 -- Escherichia coli -- heavy metal tolerance -- heavy metal‐binding -- metallothionein
Molecular biology -- Periodicals
Cytology -- Periodicals
Life sciences -- Periodicals
Biological Science Disciplines -- Periodicals
Molecular Biology -- Periodicals
Cell Biology -- Periodicals
Cytology
Life sciences
Molecular biology
Periodicals
572.805 - Journal URLs:
- http://febs.onlinelibrary.wiley.com/hub/journal/10.1002/(ISSN)2211-5463/ ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1002/2211-5463.12520 ↗
- Languages:
- English
- ISSNs:
- 2211-5463
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 8491.xml