| Identification and characterization of water stress-induced TaWSI18 gene in silico cloning from Triticum aestivum and its bioinformatic analysis |
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| DOI：10.7606/j.issn.1000-7601.2016.04.11 |
| Key Words: Triticum aestivum water stress TaWSI18 silico cloning bioinformatics |
| Author Name | Affiliation | | FAN Lei | State Key Laboratory of Crop Stress Biology in Arid Area, College of Life Sciences, Northwest A & F University, Yangling, Shaanxi 712100, China | | CHEN Juan | State Key Laboratory of Crop Stress Biology in Arid Area, College of Life Sciences, Northwest A & F University, Yangling, Shaanxi 712100, China | | ZHANG Yan-e | State Key Laboratory of Crop Stress Biology in Arid Area, College of Life Sciences, Northwest A & F University, Yangling, Shaanxi 712100, China | | ZHANG Lin-sheng | State Key Laboratory of Crop Stress Biology in Arid Area, College of Life Sciences, Northwest A & F University, Yangling, Shaanxi 712100, China | | ZHU Wei-ning | State Key Laboratory of Crop Stress Biology in Arid Area, College of Life Sciences, Northwest A & F University, Yangling, Shaanxi 712100, China | | ZHANG Da-peng | State Key Laboratory of Crop Stress Biology in Arid Area, College of Life Sciences, Northwest A & F University, Yangling, Shaanxi 712100, China |
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| Abstract: |
| WSI18, a water stress-induced genes, plays an important role in plants under water deficit. Silico cloning and RT-PCR were taken to isolate four new highly homologous WSI18 genes: TaWSI18-1, TaWSI18-2, TaWSI18-3 and TaWSI18-4 (GenBank accession number: KP226849, KP226850, KP226851and KP226852) in wheat, ORFs of which are all 678 bp encoding 225 amino acids. Bioinformatic analysis showed that they are highly hydrophilic and have multiple phosphorylation sites. They are located to cytoplasm and have no transmembrane domain signal peptides, as well as no splicing sites. The proportion of α helix and random coil are over 90% by a secondary structure prediction. Homology comparison and phylogenetic analysis showed that TaWSI18 proteins are highly homologous to WSI18 of Bromus inermis and LEA3 Brachypodium distachyon, sharing 94% and 70% similarities respectively. In addition, TaWSI18 proteins have conserved amino acid sequences common to LEA protein in the N-terminal region. They also have a similar character to LEA3 protein by bioinformatic analysis that TaWSI18 proteins may have the same or similar function to LEA3 protein, which lies a foundation for the future study on its function under water-stress. |
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