Abstract
Maize group II LEA protein ZmDHN11 could protect protein activity and confer resistance to osmotic stress on transgenic yeast and tobacco. Late embryogenesis abundant (LEA) proteins are widely assumed to play crucial roles in environmental stress tolerance, but their function has remained obscure. Dehydrins are group II LEA proteins, which are highly hydrophilic plant stress proteins. In the present study, a novel group II LEA protein, ZmDHN11, was cloned and identified from maize. The expression of ZmDHN11 was induced by high osmotic stress, low temperature, salinity, and ABA (abscisic acid). The ZmDHN11 protein specifically accumulated in the nuclei and cytosol. Further study indicated that ZmDHN11 is phosphorylated by the casein kinase CKII. ZmDHN11 protected the activity of LDH under water-deficit stress. The overexpression of ZmDHN11 endows transgenic yeast and tobacco with tolerance to osmotic stress.
Highlights
Due to global climate change, drought stress has had the most significant impact on the morphological, physiological and biochemical characteristics of plants (Jiang et al, 2013; Cai et al, 2014; Pan et al, 2012; Li et al, 2018)
In order to elucidate the role of group II Late embryogenesis abundant (LEA) proteins, ZmDHN11 (GenBank: AY103822.1) was isolated from maize
The superoxide dismutase (SOD) and POD activities in the three overexpressing lines were significantly higher than those in the WT after 1 day of drought stress. These results suggest that overexpression of ZmDHN11 improves transgenic tobacco tolerance to osmotic stress. Environmental stress, such as water deficit has a serious impact on plants (Zhang et al, 2012; Dou et al, 2015; Li et al, 2019)
Summary
Due to global climate change, drought stress has had the most significant impact on the morphological, physiological and biochemical characteristics of plants (Jiang et al, 2013; Cai et al, 2014; Pan et al, 2012; Li et al, 2018). During the evolutionary adaptation process, plants have developed a series of molecular and physiological mechanisms to reduce the damage caused by water deficit, including structural changes and the synthesis of hydrophilic proteins (Wei et al, 2016). LEA proteins were first found in cotton seeds and accumulate in the late stage of plant seed development (Dure et al, 1981). LEA proteins are mainly involved in the protection of desiccation during seed dehydration, or vegetative tissues under stress conditions by acting as cellular dewatering protectants (Wise et al, 2004). According to their conserved motifs and amino acid sequence homology, LEA proteins can be divided into seven families (Battaglia et al, 2008). The high levels of dehydrin expression enhances the ability of plants to survive abiotic stress (Malik et al, 2017)
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