Cloning, in silico characterization, subcellular localization, and expression of a heat shock cognate 70kDa protein/gene (EjHsc70-2) from Eriobotrya japonica
文献类型： 外文期刊
作者： Lin, Shoukai 1 ; Wu, Ti 2 ; Li, Ming 1 ; Huang, Xiaoming 1 ; Zhang, Yanqing 1 ; Han, Linxiao 1 ; Wu, Bisha 1 ; Chen, Yu 1 ;
作者机构： 1.Fujian Prov Univ, Key Lab Loquat Germplasm Innovat & Utilizat, Putian Univ, Putian 351100, Peoples R China
2.Dalhousie Univ, Fac Agr, Truro, NS B2N 5E3, Canada
3.Putian Univ, Fujian Prov Key Lab Ecol Toxicol Effects & Contro, Putian 351100, Peoples R China
4.Qinghai Univ, Qinghai Acad Agr & Forestry Sci, Xining 810016, Qinghai, Peoples R China
5.Fujian Agr & Forestry Univ, Overseas Educ Coll, Fuzhou 350002, Fujian, Peoples R China
6.Zhangzhou City Coll, Dept Garden & Hort, Zhangzhou 363000, Peoples R China
关键词： Loquat; EjHsc70-2; Cloning; Characterization; Subcellular localization; Expression
期刊名称：ACTA PHYSIOLOGIAE PLANTARUM （ 影响因子：2.354； 五年影响因子：2.711 ）
ISSN： 0137-5881
年卷期： 2019 年 41 卷 7 期
页码：
收录情况： SCI
摘要： Heat shock protein 70kDa proteins (Hsp70s) are among the most important molecular chaperone groups and play a significant role in the stress responses and development of plants. In the present study, the full-length cDNA of the heat shock cognate 70 protein 2 gene EjHsc70-2, which encodes a loquat Hsp70s member, was cloned and characterized, and its expression and subcellular localization were also investigated. The full-length cDNA of EjHsc70-2 consists of an open reading frame (ORF) of 1950bp, a 5-UTR of 103bp, and a 3-UTR of 62bp, and the ORF encodes 649 amino acid residues. The structure of the loquat Hsc70-2 protein was analysed using several bioinformatics tools, and the results showed that the protein was, indeed, a member of the Hsp70s. Phylogenetic tree analysis suggested that the genetic evolution of Hsc70-2 genes conformed well to the morphology based taxonomic classification of seed plants. BLAST and multiple alignment analyses determined that the Hsc70-2 genes and Hsc70-2 proteins were both highly conserved among loquat and other seed plants, suggesting that the functions of EjHsc70-2 might be similar to those of other Hsc70-2 genes. The bioinformatics and experimental subcellular localization analyses both supported that EjHsc70-2 was a cytoplasmic and/or nuclear protein. Quantitative real-time RT-PCR (RT-qPCR) suggested its conserved functions involved in loquat organ development. Moreover, EjHsc70-2 were also inducible, which may contribute to the low-temperature adaptation of loquat fruits in cold storage. These results provide new insights into the characteristics and functions of Hsp70s in Eriobotrya japonica.
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