Glycerol-3-phosphate acyltransferase is the first acyl esterifying enzyme in phosphatidylglycerol (PG) synthesis process. In this study, we isolated and characterized the glycerol-3-phosphate acyltransferase (GPAT) gene from Suaeda salsa (S. salsa) and obtained the full length of the GPAT gene from S. salsa (SsGPAT) by 5' and 3' RACE. The clone contained an open reading frame (ORF) of 1167 bp nucleotides that comprised of 388 amino acid residues. Real-time PCR revealed that the mRNA accumulation of GPAT in S. salsa was induced by salt stress. The highest expression levels were observed when S. salsa leaves were exposed to 300 mM NaCl treatment. At the germination stage, the germination rate and root length of overexpressed Arabidopsis strains were significantly higher than WT under different concentrations of NaCl treatments, while the inhibitory effect was significantly severe in T-DNA insertion mutant strains. In the seedling stage, chlorophyll content, the photochemical efficiency of PSII, PSI oxidoreductive activity (ΔI/Io) and the unsaturated fatty acid content of PG decreased less in overexpressed strains and more in mutant strains than that in WT under salt stress. These results suggest that the overexpression of SsGPAT in Arabidopsis enhances salt tolerance and alleviates the photoinhibition of PSII and PSI under salt stress by improving the unsaturated fatty acid content of PG.

Global soil salinization is increasingly a serious threat to agriculture worldwide. Therefore, it is imperative to improve crop salt tolerance as a means of adaptation to saline habitats. Some halophytes and most monocotyledonous crops are salt-excluders. Understanding the regulatory mechanisms of salt exclusion at the molecular level in salt-exclusion plants is critical for improving the salt tolerance of monocotyledonous crops such as maize, wheat, rice, and sorghum. In this review, we summarize recent research into salt-exclusion mechanisms and the genes that underlie them. Findings related to salt exclusion may accelerate the process of breeding tolerant cultivars by using genomic and molecular tools.

Plant chloroplasts have complex membrane systems. Among these, thylakoids serve as the sites for photosynthesis and photosynthesis-related adaptation. In addition to the photosynthetic membrane complexes and associated molecules, lipids in the thylakoid membranes, are predominantly composed of MGDG (monogalactosyldiacylglycerol), DGDG (digalactosyldiacylglycerol), SQDG (sulfoquinovosyldiacylglycerol) and PG (phosphatidylglycerol), play essential roles in shaping the thylakoid architecture, electron transfer, and photoregulation. In this review, we discuss the effect of abiotic stress on chloroplast structure, the changes in membrane lipid composition, and the degree of unsaturation of fatty acids. Advanced understanding of the mechanisms regulating chloroplast membrane lipids and unsaturated fatty acids in response to abiotic stresses is indispensable for improving plant resistance and may inform the strategies of crop breeding.

Small peptides in plants are typically characterized as being shorter than 120 amino acids, with their biologically active variants comprising fewer than 20 amino acids. These peptides are instrumental in regulating plant growth, development, and physiological processes, even at minimal concentrations. They play a critical role in long-distance signal transduction within plants and act as primary responders to a range of stress conditions, including salinity, alkalinity, drought, high temperatures, and cold. This review highlights the crucial roles of various small peptides in plant growth and development, plant resistance to abiotic stress, and their involvement in long-distance transport. Furthermore, it elaborates their roles in the regulation of plant hormone biosynthesis. Special emphasis is given to the functions and mechanisms of small peptides in plants responding to abiotic stress conditions, aiming to provide valuable insights for researchers working on the comprehensive study and practical application of small peptides.