» Articles » PMID: 37837550

The Thioredoxin H-type TdTrxh2 Protein of Durum Wheat Confers Abiotic Stress Tolerance of the Transformant Arabidopsis Plants Through Its Protective Role and the Regulation of Redox Homoeostasis

Overview
Journal Protoplasma
Publisher Springer
Specialty Biology
Date 2023 Oct 14
PMID 37837550
Authors
Affiliations
Soon will be listed here.
Abstract

The thioredoxins (Trxs) are ubiquitous and they play a crucial role in various biological processes like growth and stress response. Although the functions of Trxs proteins are described in several previous reports, the function of the isoform Trxh2 of durum wheat (Triticum durum L.), designated as TdTrxh2, in abiotic stress response still unknown. Thus, we aimed in this study the functional characterization of TdTrxh2 through its expression in yeast cells and Arabidopsis plants. Sequence analysis revealed that TdTrxh2 protein shared the conserved redox site with the other Trxh from other plant species. Under various abiotic stresses, TdTrxh2 was up-regulated in leaves and roots of durum wheat. Interestingly, we demonstrated that TdTrxh2 exhibit protective effect on LDH activity against various treatments. Besides, the expression of TdTrxh2 in yeast cells conferred their tolerance to multiple stresses. Moreover, transgenic Arabidopsis expressing TdTrxh2 showed tolerance phenotype to several abiotic stresses. This tolerance was illustrated by high rate of proline accumulation, root proliferation, low accumulation of reactive oxygen species like HO and O, and high antioxidant CAT and POD enzymes activities. All these findings suggested that TdTrxh2 promotes abiotic stress tolerance through the redox homoeostasis regulation and its protective role.

References
1.
Arsova B, Hoja U, Wimmelbacher M, Greiner E, Ustun S, Melzer M . Plastidial thioredoxin z interacts with two fructokinase-like proteins in a thiol-dependent manner: evidence for an essential role in chloroplast development in Arabidopsis and Nicotiana benthamiana. Plant Cell. 2010; 22(5):1498-515. PMC: 2899873. DOI: 10.1105/tpc.109.071001. View

2.
Beyer Jr W, Fridovich I . Assaying for superoxide dismutase activity: some large consequences of minor changes in conditions. Anal Biochem. 1987; 161(2):559-66. DOI: 10.1016/0003-2697(87)90489-1. View

3.
Bradford M . A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976; 72:248-54. DOI: 10.1016/0003-2697(76)90527-3. View

4.
Cazalis R, Pulido P, Aussenac T, Perez-Ruiz J, Cejudo F . Cloning and characterization of three thioredoxin h isoforms from wheat showing differential expression in seeds. J Exp Bot. 2006; 57(10):2165-72. DOI: 10.1093/jxb/erj174. View

5.
Chibani K, Wingsle G, Jacquot J, Gelhaye E, Rouhier N . Comparative genomic study of the thioredoxin family in photosynthetic organisms with emphasis on Populus trichocarpa. Mol Plant. 2009; 2(2):308-22. DOI: 10.1093/mp/ssn076. View