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作 者:刘娟 朱春晓 肖雪琼[1] 莫陈汨 王高峰[1] 肖炎农[1] LIU Juan;ZHU Chun-xiao;XIAO Xue-qiong;MO Chen-mi;WANG Gao-feng;XIAO Yan-nong(College of Plant Science and Technology,Huazhong Agricultural University,Wuhan 430070)
机构地区:[1]华中农业大学植物科学技术学院,武汉430070
出 处:《生物技术通报》2021年第7期137-145,共9页Biotechnology Bulletin
基 金:国家自然科学基金项目(31872019);江西省重点研发计划项目(20181ACF60018)。
摘 要:以淡紫紫孢菌中参与盐胁迫响应的亲环蛋白PlCYP6为研究对象,采用免疫沉淀联合质谱分析及酵母双杂交等技术筛选淡紫紫孢菌中与PlCYP6互作的蛋白。结果显示,受PlCYP6特异钓取的482个蛋白的功能主要涉及细胞代谢。其中,乙醇脱氢酶1(alcohol dehydrogenase I,ADH1)与PlCYP6直接互作,且PlCYP6的WD40 repeat结构域为二者间互作的关键区域。同时,PlCYP6和ADH1均受NaCl胁迫诱导表达。上述研究结果表明,ADH1为PlCYP6的候选互作蛋白,这为进一步解析淡紫紫孢菌响应盐胁迫机制奠定了基础。The cyclophilin PlCYP6 that is involved in the responses of Purpureocillium lilacinum to salt stresses was used as the research object,and the putative interaction protein of PlCYP6 in P.lilacinum was screened using immunoprecipitation combined with mass spectrometry(IP-MS),yeast two-hybrid assay and other techniques.Results indicated that 482 proteins was specially fished by PlCYP6,and mainly functioned in cell metabolism.Among them,alcohol dehydrogenase 1(ADH1)directly interacted with PlCYP6,and the domain,WD40 repeat,of PlCYP6 was involved the interaction between them.Meanwhile,both PlCYP6 and ADH1 were induced by NaCl stress.These findings reveal that ADH1 is a putative interaction protein of PlCYP6,which lays a foundation for further uncovering the mechanism of responses of P.lilacinum to salt stresses.
关 键 词:淡紫紫孢菌 PlCYP6 盐胁迫应激反应 免疫沉淀联合质谱 互作蛋白
分 类 号:S476.1[农业科学—农业昆虫与害虫防治]
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