Systematic identification and analysis of the HSP70 genes reveals MdHSP70-38 enhanced salt tolerance in transgenic tobacco and apple

Int J Biol Macromol. 2024 Dec 17:289:138943. doi: 10.1016/j.ijbiomac.2024.138943. Online ahead of print.

Abstract

Heat shock protein 70 (HSP70) is a class of important molecular chaperones that are involved in protein folding, stabilization, and maturation, and play a vital role in plant growth and response to environmental stress. Apple trees frequently suffer from different-degree salt stress, which seriously affects their growth, quality, and yield. However, whether HSP70 genes are involved in salt tolerance is unexplored in apple. In this study, 67 MdHSP70 genes were identified and unevenly distributed on 17 apple chromosomes. Gene structure and protein motif analysis revealed that MdHSP70 genes in the same subgroup have similar intron phase and motif organization, further supporting the phylogenetic results. RNA-seq analysis showed the expression level of nine of 67 MdHSP70 genes was induced by salt stress. Subsequent qRT-PCR analysis revealed that MdHSP70-38 was dramatically up-regulated in response to salt stress. The overexpression of MdHSP70-38 in transgenic tobacco and apple improved salt stress tolerance, which was associated with less electrolyte leakage and malondialdehyde (MDA), as well as diminished accumulation of hydrogen peroxide (H2O2) and superoxide radicals (O2-). Our findings demonstrated that MdHSP70-38 played a positive regulatory role in salt tolerance in tobacco and apple, and provided a promising candidate gene in genetic applications for improving salt tolerance.

Keywords: Apple; Expression analysis; Function identification; Heat shock protein; Salt stress.