Acta Agrestia Sinica ›› 2018, Vol. 26 ›› Issue (5): 1181-1189.DOI: 10.11733/j.issn.1007-0435.2018.05.021

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Analysis of Salt Tolerance Function of Protein Disulfide Isomerase Gene Family in Zoysia matrella

XIAO Xiao-lin, WANG Kai, ZHANG Bing, LIU Jian-xiu   

  1. Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, Jiangsu Province 210014, China
  • Received:2018-05-15 Revised:2018-09-02 Online:2018-10-15 Published:2018-11-06

沟叶结缕草蛋白质二硫键异构酶(ZmPDIs)基因家族耐盐功能分析

肖晓琳, 王凯, 张兵, 刘建秀   

  1. 江苏省中国科学院植物研究所, 江苏 南京 210014
  • 通讯作者: 张兵, 刘建秀
  • 作者简介:肖晓琳(1993-),女,河南洛阳人,硕士研究生,主要从事园艺植物抗逆性分子研究,E-mail:hilda_512@foxmail.com
  • 基金资助:
    国家自然科学基金(31672195,31572155)项目资助

Abstract: Protein disulfide isomerase (PDI) and PDI-like proteins (PDILs),belonging to thioredoxin (Trx) superfamily,have diverse functions in organisms. PDI/PDIL can not only catalyze thiol-disulfide interchange,resulting in the formation,reduction,or isomerization of protein disulfide bonds in protein substrates,but also display chaperone activity. Furthermore,PDI/PDIL also have Ca2+-binding domain. This study identified 5 ZmPDI genes in Zoysia matrella. Phylogenetic and structural analyses of these genes were conducted,and used salinity-sensitive yeast mutants to verify their salt tolerance. Real-time PCR result showed that PDIs displayed up-regulation in response to NaCl treatments. Our result provided an important reference for further study of salt tolerance's physiological function and molecular mechanism of Zoysia matrella.

Key words: Protein disulfide isomerase, Zoysia matrella, Phylogenetic analysis, Gene expression profiling

摘要: 蛋白质二硫键异构酶(protein disulfide isomerase,PDI)及其类蛋白,是硫氧还蛋白超家族的重要成员,具有分子伴侣活性及钙离子结合位点,负责催化蛋白质二硫键的氧化、还原和异构。本研究从沟叶结缕草基因组中鉴定获得了5个蛋白质二硫键异构酶(ZmPDIs)基因,对其进行了系统进化与基因结构的生物信息学分析,利用同源基因缺失酵母突变体对其耐盐功能进行了初步分析。荧光定量RT-PCR结果表明5个ZmPDIs基因的表达均受到盐胁迫的诱导。这些结果为进一步研究ZmPDIs的耐盐生理功能及分子机制提供参重要参考。

关键词: 蛋白质二硫键异构酶, 沟叶结缕草, 生物信息学分析, 基因表达

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