Titlebar

Export bibliographic data
Literature by the same author
plus on the publication server
plus at Google Scholar

 

Identification of C-terminal Regions in Arabidopsis Thaliana Phytochelatin Synthase 1 Specifically Involved in Activation by Arsenite

Title data

Uraguchi, Shimpei ; Sone, Yuka ; Ohta, Yumika ; Ohkama-Ohtsu, Naoko ; Hofmann, Christian ; Hess, Natalia ; Nakamura, Ryosuke ; Takanezawa, Yasukazu ; Clemens, Stephan ; Kiyono, Masako:
Identification of C-terminal Regions in Arabidopsis Thaliana Phytochelatin Synthase 1 Specifically Involved in Activation by Arsenite.
In: Plant & Cell Physiology. Vol. 59 (2018) Issue 3 . - pp. 500-509.
ISSN 1471-9053
DOI: https://doi.org/10.1093/pcp/pcx204

Abstract in another language

Phytochelatins (PCs) are major chelators of toxic elements including inorganic arsenic (As) in plant cells. Their synthesis confers tolerance and influences within-plant mobility. Previous studies had shown that various metal/metalloid ions differentially activate PC synthesis. Here we identified C-terminal parts involved in arsenite- [As(III)] dependent activation of AtPCS1, the primary Arabidopsis PC synthase. The T-DNA insertion in the AtPCS1 mutant cad1-6 causes a truncation in the C-terminal regulatory domain that differentially affects activation by cadmium (Cd) and zinc (Zn). Comparisons of cad1-6 with the AtPCS1 null mutant cad1-3 and the double mutant of tonoplast PC transporters abcc1/2 revealed As(III) hypersensitivity of cad1-6 equal to that of cad1-3. Both cad1-6 and cad1-3 showed increased As distribution to shoots compared with Col-0, whereas Zn accumulation in shoots was equally lower in cad1-6 and cad1-3. Supporting these phenotypes of cad1-6, PC accumulation in the As(III)-exposed plants were at trace level in both cad1-6 and cad1-3, suggesting that the truncated AtPCS1 of cad1-6 is defective in PCS activity in response to As(III). Analysis of a C-terminal deletion series of AtPCS1 using the PCS-deficient mutant of fission yeast suggested important regions within the C-terminal domain for As(III)-dependent PC synthesis, which were different from the regions previously suggested for Cd- or Zn-dependent activation. Interestingly, we identified a truncated variant more strongly activated than the wild-type protein. This variant could potentially be used as a tool to better restrict As mobility in plants.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: BAYCEER144393
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Plant Physiology
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Plant Physiology > Chair Plant Physiology - Univ.-Prof. Dr. Stephan Clemens
Research Institutions
Research Institutions > Research Centres
Research Institutions > Research Centres > Bayreuth Center of Ecology and Environmental Research- BayCEER
Result of work at the UBT: Yes
DDC Subjects: 500 Science
Date Deposited: 05 Apr 2019 10:28
Last Modified: 05 Apr 2019 10:28
URI: https://eref.uni-bayreuth.de/id/eprint/48275