DICP OpenIR
学科主题物理化学
Identification of S-adenosyl-l-methionine synthetase as an interaction partner of an oligochitosan-induced protein kinasein tobacco in the yeast two-hybrid system
Yang JL(杨金丽); Zhao XM(赵小明); Ma XJ(马小军); Du YG(杜昱光)
会议名称The 13th International Biotechnology Symposium
会议日期2008-10-12
2008-10-12
会议地点中国
页码S581/2
部门归属十八室
主办者中国科学院 中国工程院 中华人民共和国教育部 中华人民共和国科学技术部 中华人民共和国国家发展改革委员会
英文摘要Recent reports have shown that oligochitosan elicitors can elicit multiple resistance response in plants (Yamaguchi et al., 2000). In the present study, an oligochitosan-induced protein kinase (OIPK) was found to be involved in the signal pathway of oligochitosaninduced defense reactions in tobacco (Feng et al., 2006). To further investigate how OIPK functions in the signal transduction, yeast two-hybrid screening was performed to find its interaction partners. The pGBKT7-OIPKL plasmid was used as bait to screen a tobacco BY-2 cell suspension library (Calderini et al., 2001)constructed in the CLONTECH activation domain vector pACT2 according to the CLONTECH matchmaker two-hybrid systemprotocol. Positive plasmidswere then sequenced and blasted inNCBI. The C-terminal part of an S-adenosyl-l-methionine synthetase (SAMS) was identified to be interacted with OIPKL in the yeast twohybrid system. SAMS catalyses the conversion of methionine to S-adenosylmethionine (SAM), which is the major methyl group donor in living organisms. SAMS was reported to be involved in fungal elicitor induced pathogen defense in Petroselinum crispurm (Kawalleck et al., 1992). The full length of SAMS was then cloned from tobacco and further analysis indicate that SAMS specifically interacts with the 316–500 amino acid of OIPKL protein in yeast. Further investigations are in progress in our lab to prove this interaction and to find out how they functions in oligochitosan induced plant resistance.
语种中文
文献类型会议论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/113228
专题中国科学院大连化学物理研究所
通讯作者Du YG(杜昱光)
推荐引用方式
GB/T 7714
Yang JL,Zhao XM,Ma XJ,et al. Identification of S-adenosyl-l-methionine synthetase as an interaction partner of an oligochitosan-induced protein kinasein tobacco in the yeast two-hybrid system[C],2008:S581/2.
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