Heat shock factor ZmHsf17 positively regulates phosphatidic acid phosphohydrolase ZmPAH1 and enhances maize thermotolerance.

Abstract

Heat stress adversely impacts plant growth, development, and grain yield. Heat shock factors (Hsf), especially the HsfA2 subclass, play a pivotal role in the transcriptional regulation of genes in response to heat stress. In this study, the coding sequence of maize ZmHsf17 was cloned. ZmHsf17 contained conserved domains including a DNA binding domain, oligomerization domain, and transcriptional activation domain. The protein was nuclear localized and had transcription activation activity. Yeast two-hybrid and split luciferase complementation assays confirmed the interaction of ZmHsf17 with members of the maize HsfA2 subclass. Overexpression of ZmHsf17 in maize significantly increased chlorophyll content and net photosynthetic rate, and enhanced the stability of cellular membranes. Through integrative analysis of ChIP-seq and RNA-seq datasets, ZmPAH1, encoding phosphatidic acid phosphohydrolase of lipid metabolic pathways, was identified as a target gene of ZmHsf17. The promoter fragment of ZmPAH1 was bound by ZmHsf17 in protein-DNA interaction experiments in vivo and in vitro. Lipidomic data also indicated that the overexpression of ZmHsf17 increased levels of some critical membrane lipid components of maize leaves under heat stress. This research provides new insights into the role of the ZmHsf17-ZmPAH1 module in regulating thermotolerance in maize.