Abstract

Plant heat stress transcription factors (Hsfs) belong to a very large gene family and play dominant roles in response to heat stress. Here, we report the functional analysis of VaHsfC1, a class C Hsf gene from Vitis amurensis, and involved in multiple abiotic stresses. The structure of VaHsfC1 contains a typical HSF domain for DNA-binding at N terminus. Phylogenetic analysis revealed that VaHsfC1 belongs to the C1 family of Hsfs. VaHsfC1 was highly induced by heat, cold, exogenous abscisic acid (ABA) and salinity, respectively. Unusually, VaHsfC1was preferentially localized in nucleus, but less in the cytosol. Also, no transcriptional activation was detected for the protein in yeast cells. Ectopic VaHsfC1 expression in Arabidopsis enhanced heat tolerance characterized by the increased survival rate, higher chlorophyll content, reduced electrolyte leakage, and activated expressions of ascorbate peroxidase (Apx2) and heat shock protein (HSP) expression compared to the WT. Interestingly, overexpression of VaHsfC1 in Arabidopsis could also increase the cold tolerance, as reveled from a series changes at the physiological and biochemical steps, as well as at the transcript levels of CORs in the CBF-dependent responsive pathway. Additionally, the growth of VaHsfC1-overexpressing Arabidopsis showed enhanced seed ABA hypersensitivity during germination and cotyledon development, and a significant reduction in stomatal aperture was also observed in overexpression lines. Furthermore, VaHsfC1-overexpressing lines displayed salt-hypersensitive phenotype with a lower rates both in germination and cotyledon greening, and the inhibition of root growth. Our findings demonstrated that the complex nature of VaHsfC1 in mediating multiple abiotic stress responses, as a key component to further understanding of the ‘crosstalk’ mechanism of multiple abiotic stress response in plants.

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.