Elucidating the functional role of heat stress transcription factor A6b (TaHsfA6b) in linking heat stress response and the unfolded protein response in wheat.

KEY MESSAGE: TaHsfA6b-4D relocalizes intracellularly upon heat stress and play a significant role in linking the heat stress response to unfolded-protein response so as to maintain cellular homeostasis. Heat stress transcription factors (Hsfs) play a crucial role in protecting the plants against heat stress (HS). In case of wheat, TaHsfA6b-4D (earlier known as TaHsfA2d) has been identified as a seed preferential transcription factor and its role has been shown in various abiotic stresses such as heat, salt and drought stress. In the present study, a homeologue of TaHsfA6b gene (TaHsfA6b-4A) was identified and was found to be transcriptionally inactive but it localized to the nucleus. Interestingly, TaHsfA6b-4D localized to the endoplasmic reticulum-Golgi complex and peroxisomes under non-stress conditions, but was observed to accumulate in the nucleus upon HS. The expression of TaHsfA6b-4D was upregulated by dithiothreitol (DTT), which is a known ER stress inducer. Consistent with this, Arabidopsis transgenic plants overexpressing TaHsfA6b-4D performed better on DTT containing media, which further corroborated with the increased expression of ER stress marker genes in these transgenic plants in comparison to the wild type plants. Thus, these studies together suggest that TaHsfA6b-4D may relocalize intracellularly upon heat stress and may play a significant role in linking the unfolded-protein response with heat stress response so as to maintain protein homeostasis inside the cell under heat stress.