RIBONUCLEASE AND ITS INHIBITOR FROM BACILLUS AMYLOLIQUENFACIENS

芽孢杆菌的胞外核糖核酸酶Barnase Amyloliquefaciens及其胞内抑制物Barstar被用作 蛋白质折叠和蛋白质-蛋白质研究的模型系统 互动。Barnase是核糖核酸酶的同源基团之一 存在于原核生物和真核生物中。 重组DNA技术正在应用于该项目，有三个 主要目标：1)促进生产，2)审查结构和 基因的控制序列和3)量身定做 对序列进行修改，以测试蛋白质折叠理论。 Barnase基因携带一个失活转座子和一个片段 与转座子插入位点重叠的野生型基因已被克隆 在原核表达载体中。重建表明，本地基因是 在大肠杆菌中是致命的。整个基因已经被测序，证实了 氨基酸序列，并揭示了典型的出口信号序列 蛋白质。这个残缺的基因在大肠杆菌和枯草杆菌中都有转录。

Two proteins, barnase, the extracellular ribonuclease of Bacillus amyloliquefaciens, and barstar, its intracellular inhibitor, are used as a model system for the study of protein folding and protein-protein interactions. Barnase is one of an homologous group of ribonucleases occurring in both prokaryotes and eukaryotes. Recombinant DNA techniques are being applied to the project with three major aims; 1) to facilitate production, 2) to examine the structural and control sequences of the genes and 3) to tailor specifically designed modifications in the sequences to test theories of protein folding. The barnase gene carrying an inactivating transposon and a fragment of the wild type gene overlapping the transposon insertion site have been cloned in E. coli plasmids. Reconstructions demonstrate that the native gene is lethal in E. coli. The entire gene has been sequenced, confirming the amino acid sequence and revealing a signal sequence typical of exported proteins. The crippled gene is transcribed in both E. coli and B. subtilis.