Abstract
Aquaporins are known as water channel proteins. In this study, an aquaporin gene MdPIP1;2 was cloned from Malus domestica cv. Qinguan encoding a protein of 289 amino acids that formed the typical structure of aquaporin by six transmembrane domains, two asparagine–proline–alanine motifs, aromatic/arginine filter, and Forger's position. MdPIP1;2 was highly expressed in the water-sensitive or water-requiring tissues, and upregulated by salt and PEG stresses. MdPIP1;2 transgenic Arabidopsis exhibited enhanced salt stress tolerance with less Na + accumulation, lower malondialdehyde (MDA) content, lower electrolyte leakage (EL) level, and higher superoxide dismutase (SOD) and peroxidase (POD) activities compared with WT plants. Additionally, transcriptome analysis indicated MdPIP1;2 transgenic Arabidopsis could present healthier growth and development condition probably through regulating morphological structures and accumulating specific secondary metabolites under salt stress. Our results are a useful reference for better understanding the biological function of aquaporin in apple tree, especially in plant response to abiotic stress.
Published Version
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