巴西固氮螺菌中杂合双组分蛋白Org35与NifA的相互作用  

The Interaction between NifA and Hybrid Two Component Protein Org35 of Azospirillum brasilense

作　　者：崔艳华[1,2] 伍丽娴[1] 洪媛媛[1] 陈三凤[1] 

机构地区：[1]中国农业大学农业生物技术国家重点实验室,北京100094 [2]哈尔滨工业大学食品科学与工程学院,哈尔滨150090

出　　处：《农业生物技术学报》2010年第3期580-585,共6页Journal of Agricultural Biotechnology

基　　金：国家自然科学基金资助项目(30470028)资助

摘　　要：巴西固氮螺菌(Azospirillum brasilense)可以与玉米(Zea mays)、小麦(Triticum aestivum)等重要作物联合固氮,是重要的潜在生物肥料。NifA蛋白是所有固氮基因转录所必需的激活蛋白。本研究利用融合蛋白下拉分析,探讨了Org35蛋白与NifA蛋白的相互作用。研究表明二者存在互作。Org35蛋白由3个独立结构区域组成,即PAS结构域、组氨酸蛋白激酶结构域和应答调节蛋白区域。本研究采用融合蛋白下拉分析了Org35蛋白三个结构域与NifA的互作关系,结果表明Org35蛋白与NifA蛋白之间的相互作用是由PAS结构域介导的。Azospirillum brasilense is a nitrogen fixing bacteria with roots of several important cereals such as maize, wheat and rice, and may be used as a potential biofertilizer. NifA is a common transcriptional activator for the nitrogen fixation gene. The interaction between Org35 and NifA was studied by means of fusion protein pull-down analysis. The results indicated the two proteins have interaction each other. Org35 was consisted of three domains, including PAS domain, histidine protein kinase domain （HPK）, and receive receptor domain （RR）. The interactions between the three domains of Org35 and NifA were studied. The results indicated the interaction between Org35 and NifA was mediated by PAS domain.

关 键 词：巴西固氮螺菌 NIFA蛋白 PAS结构域 杂合双组分蛋白 融合蛋白下拉 

分 类 号：Q936[生物学—微生物学]