An aquaporin gene MdPIP1;2 from Malus domestica confers salt tolerance in transgenic Arabidopsis.

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.