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农垦58s育性转换期间叶片核蛋白因子与LRE结合研究
引用本文:杨代常,徐平,朱英国.农垦58s育性转换期间叶片核蛋白因子与LRE结合研究[J].武汉大学学报(理学版),1995(6).
作者姓名:杨代常  徐平  朱英国
作者单位:武汉大学生命科学学院
摘    要:运用人工合成的LRE序列,采用Bandshiftassay方法分析了农垦58s和农垦58品种叶片中核蛋白因子与LRE的结合反应.研究结果表明:在农垦58S的育性转换敏感期叶片中存在与LRE结合的核蛋白因子,这种核蛋白因子受磷酸化的调节;认为在长日照下农垦58s叶片中的核蛋白因子以磷酸化的形式与LRE结合,磷酸化促进了核蛋白二聚化过程.同时比较了农垦58s和农垦58品种叶片中核蛋白因子与LRE结合反应的差别,二者的叶片中的核蛋白不仅与LRE的结合活性存在差异,而且其调节方式明显不同.

关 键 词:PGMR,LRE-核蛋白结合反应,核蛋白磷酸化,Bandshiftassay

THE STUDY ON THE SPECIFIC INTERACTION BETWEEN LRE AND NUCLEAR PROPEINS OF LEAVES IN PGMR DURING FERTILITY TRANSFORMATION
Yang Daichang,Xu Ping,Zhu Yingguo.THE STUDY ON THE SPECIFIC INTERACTION BETWEEN LRE AND NUCLEAR PROPEINS OF LEAVES IN PGMR DURING FERTILITY TRANSFORMATION[J].JOurnal of Wuhan University:Natural Science Edition,1995(6).
Authors:Yang Daichang  Xu Ping  Zhu Yingguo
Abstract:We analysed the binding intereaction of nuclear proteins of leaves in Nongken 58 s and Nongken 58 variety by Bandshift assay, using a 37 hp synthetic LRE from rbcs genes. The results indicated that the nuclear proteins specifically binding to LRE existed in the two varieties in leaves during fertility transformation. The binding activity is stimulated by phosphorylation of the nuclear proteins,meanwhile,the stimulation accompanied with disappearing and weakening of another binding band. It suggested that the nuclear proteins in leaves of Nongken 58 s Under longday may be dimer of the nuclear proteins specifically binding to LRE, which are regulated by phosphorylatin. The comparison of interaction of the nuclear proteins with LRE between Nongken 58 s and Nongken 58 variety indicated that they were not only different from the binding bands, but also different from the regulation pattern.
Keywords:PGMR  intereaction of LRE-nuclear protein  phosphorylation  bandshift assay
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