Abstract
Maize (Zea mays) is a major cereal crop worldwide, and there is increasing demand for maize cultivars with enhanced tolerance to desiccation. Late embryogenesis abundant (LEA) proteins group 5C is involved in plants’ responses to various osmotic stresses such as drought and salt. A putative group 5C LEA gene from Z. mays cv. Tevang 1 was isolated, named ZmLEA14tv, and cloned into a T-DNA for expression in plants. The deduced amino acid of ZmLEA14tv showed a conserved Pfam LEA_2 domain and a high proportion of hydrophobic residues, characteristic of group 5C LEA proteins. Transgenic tobacco and maize plants expressing ZmLEA14tv were generated. During drought simulation conditions, the ZmLEA14tv-expressing plants of tobacco showed improved recovery ability, while those of maize enhanced the seed germination in comparison with the non-transgenic control plants. In addition, the survival rate of ZmLEA14tv transgenic maize seedlings was twice as high as the control. These results indicated that ZmLEA14tv might be involved in the drought tolerance of plants and could be a candidate gene for developing enhanced drought-tolerant crops.
Highlights
Late embryogenesis abundant (LEA) proteins are mostly hydrophilic proteins, which can reduce the damage caused by severe environmental conditions
The isolated ZmLEA14tv had a size of 693 base pairs with an open reading frame of 459 bp in length encoding for a deduced 152 amino acid protein
The present study showed that the expression of ZmLEA14tv in tobacco significantly improved the recoverability of transgenic plants suffering from a short desiccation (Figure 2)
Summary
Late embryogenesis abundant (LEA) proteins are mostly hydrophilic proteins, which can reduce the damage caused by severe environmental conditions. LEA proteins were reported to contribute to various developmental processes and to accumulate in response to drought, low temperature, salt stress, or treatment with the phytohormone ABA [1,2,3,4]. LEA proteins accumulated during the late stages of embryogenesis and associated with the desiccation of seeds’ embryos [7,8]. The LEA proteins of groups 1, 2, 3, 4, 6, and 7 are hydrophilic or typical LEA proteins, which have a low proportion of cysteine and tryptophan residues, and a high proportion of glycine, glutamic acid, lysine, and threonine residues. The group 5 LEA protein has high content of hydrophobic residues. Based on amino acid sequences and conserved motifs, the group 5 LEA protein
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