Létoffé S, Delepelaire P, Wandersman C
Unité de Génétique Moléculaire, Institut Pasteur, Paris, France.
Mol Microbiol. 1989 Jan;3(1):79-86. doi: 10.1111/j.1365-2958.1989.tb00106.x.
Erwinia chrysanthemi, a phytopathogenic bacterium, produces a protease inhibitor which is a low-molecular-weight, heat-stable protein. In addition to its action on the three E. chrysanthemi extracellular proteases A, B and C, it also strongly inhibits the 50 kD extracellular protease of Serratia marcescens. Its structural gene (inh) was subcloned and expressed in Escherichia coli, in which it encodes an active inhibitor which was purified. The nucleotide sequence of the inh gene shows an open reading frame of 114 condons. The N-terminal amino acid sequence of the purified inhibitor was also determined. It indicated the existence of an amino-terminal signal peptide absent from the mature protein. The inhibitor is entirely periplasmic in E. chrysanthemi and partially periplasmic in E. coli.
菊欧文氏菌是一种植物致病细菌，它能产生一种蛋白酶抑制剂，该抑制剂是一种低分子量、热稳定的蛋白质。除了对菊欧文氏菌的三种细胞外蛋白酶A、B和C有作用外，它还能强烈抑制粘质沙雷氏菌的50 kD细胞外蛋白酶。其结构基因（inh）被亚克隆并在大肠杆菌中表达，在大肠杆菌中它编码一种活性抑制剂并被纯化。inh基因的核苷酸序列显示有一个114个密码子的开放阅读框。还测定了纯化抑制剂的N端氨基酸序列。结果表明成熟蛋白中不存在氨基端信号肽。该抑制剂在菊欧文氏菌中完全位于周质，在大肠杆菌中部分位于周质。
