Overexpression of Prunus mume Dehydrin Genes in Tobacco Enhances Tolerance to Cold and Drought.

Fei Bao,Yang An,Dongliang Du,Qixiang Zhang,Weiru Yang,Jia Wang,Tangren Cheng

doi:10.3389/fpls.2017.00151

Abstract

Dehydrins, known as group 2 or D-11 family late-embryogenesis-abundant (LEA) proteins, play important roles in plant growth and stress tolerance. Six dehydrin genes were previously identified from the genome of Prunus mume. In this study, five of them (PmLEA8, PmLEA10, PmLEA19, PmLEA20, and PmLEA29) were cloned from cold-resistant P. mume ‘Beijingyudie’. Real-time RT-PCR analysis indicated that all these genes could be up-regulated by one or several treatments (ABA, SA, low temperature, high temperature, PEG, and NaCl treatments). The results of spot assay demonstrated that the expression of all these dehydrins, except PmLEA8, conferred improved osmotic and freezing-resistance to the recombinant Escherichia coli. So four dehydrin genes, PmLEA10, PmLEA19, PmLEA20 and PmLEA29 were chosen for individual over-expression in tobacco plants. The transgenic tobacco plants showed lower relative content of malondialdehyde, relative electrolyte leakage and higher relative content of water than control plants when exposed to cold and drought stress. These results demonstrated that PmLEAs were involved in plant responses to cold and drought.

Highlights

Dehydrins, which are known as group 2 or D-11 family late-embryogenesis-abundant (LEA) proteins, are a family of highly hydrophilic, glycine-rich, heat-stable, and intrinsically unstructured proteins (Soulages et al, 2003; Hundertmark and Hincha, 2008; Banerjee and Roychoudhury, 2016)
According to a previous bioinformatics analysis (Du et al, 2013), six dehydrin genes were identified from P. mume: PmLEA8, PmLEA9, PmLEA10, PmLEA19, PmLEA20, and PmLEA29
Except PmLEA9 were cloned from the chosen variety ‘Beijingyudie’ (Figure 1b)

Summary

Introduction

Dehydrins, which are known as group 2 or D-11 family late-embryogenesis-abundant (LEA) proteins, are a family of highly hydrophilic, glycine-rich, heat-stable, and intrinsically unstructured proteins (Soulages et al, 2003; Hundertmark and Hincha, 2008; Banerjee and Roychoudhury, 2016). They have been reported in a wide range of organisms, including higher plants, mosses, fungi, algae, and cyanobacteria (Close and Lammers, 1993; Cuming et al, 1994; Li et al, 1997; Saavedra et al, 2006; Pochon et al, 2013). Based on the arrangement of these three segments, dehydrins can be classified into five subclasses: YnSKn, SKn, Kn, YnKn, and KnS (Close, 1996, 1997)

Methods

Results

Discussion

Conclusion