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Comparative transcriptome analysis of the calcium signaling and expression analysis of sodium/calcium exchanger in Aspergillus cristatus
- Ren, Xiu‐xiu, Wang, Yuchen, Liu, YongXiang, Tan, Yumei, Ren, Chunguang, Ge, Yongyi, Liu, Zuoyi
- Journal of basic microbiology 2018 v.58 no.1 pp. 76-87
- Aspergillus, amino acids, calcium, calcium signaling, databases, gene expression, gene expression regulation, genes, hyphae, ions, open reading frames, proteins, salt stress, sexual development, sodium, sodium chloride, transcriptomics, yeasts
- Aspergillus cristatus develops into various stages under different Na concentrations: the sexual stage in 0.5 M NaCl and asexual development stage in 3 M NaCl. In order to explore whether the Ca²⁺ signaling pathway in A. cristatus responded to the changes in the salt stress, we analyzed the gene expression levels in A. cristatus respectively cultured in 0.5 M NaCl and 3 M NaCl. According to the BLAST analysis results, we identified 25 Ca²⁺‐signaling proteins in A. cristatus. The expression levels of most genes involved in the Ca²⁺‐signaling pathway in A. cristatus cultured in different salt concentrations showed significant differences, indicating that the Ca²⁺ signaling pathway was involved in the response to the changes in the salt stress. In yeasts, only calcium ion influx proteins were reported to be involved in the response to the changes in the salt stress. So far, the protein for the exchanger of calcium/sodium ions has not been reported. Therefore, we obtained the sodium/calcium exchanger (termed NCX) proteins from the KEGG Database. The ncx gene of A. cristatus was cloned and characterized. The full length of ncx gene is 3055 bp, including a 2994‐bp open reading frame encoding 994 amino acids. The expression levels of ncx in the sexual development stage and asexual development stage were respectively ∼8.94 times and ∼2.57 times of that in the hyphal formation stage. Therefore, we suggested that ncx gene was up‐regulated to resist the sodium stress. The study results provide the basis for further exploring the Ca²⁺‐signaling mechanism and ion exchanger mechanism.