Decoding the role of durum wheat ascorbate peroxidase TdAPX7B-2 in abiotic stress response.

APX proteins are HO-scavenging enzymes induced during oxidative stress. In the first part of this study, we provided an extensive knowledge on the APX family of Triticum durum, TdAPX and their related TdAPX-R, via the genome wide analysis. The outcomes showed that these proteins are clustered into four major subgroups. Furthermore, the exon-intron structure and the synteny analyses revealed that during evolution the genes TdAPX and TdAPX-R are relatively conserved. Besides, during their evolution, these genes underwent purifying selection pressure and were duplicated in segmental. In parallel, the analysis of the conserved motifs and the multiple sequence alignment demonstrated that the residues involved in the active sites, heme- and cations-binding are conserved only in TdAPX proteins. Following the RNA-seq data and the regulatory elements analyses, we focused in the second part of this study on the functional characterization of TdAPX7B-2. The qRT-PCR data showed the upregulation of TdAPX7B-2 essentially in leaves of durum wheat exposed to salt, cold, drought, metals and ABA treatments. The tolerance phenotype of the TdAPX7B-2-expressing Arabidopsis lines to salt, direct-induced oxidative stress and heavy metals was manifested by the development of root system, proline accumulation and induction of the antioxidant CAT, SOD and POD enzymes to maintain the non-toxic HO levels. Likewise, the response to salt stress and direct-oxidative stress of the transgenic lines was accompanied mainly by the induction of AtNCED3, AtRD29A/B and AtERD1.