Heiman C, Miller C G
J Bacteriol. 1978 Aug;135(2):588-94. doi: 10.1128/jb.135.2.588-594.1978.
Mutants of Salmonella typhimurium lacking protease II, an endoprotease with trypsin-like specificity, have been isolated. These mutants can be identified by using the chromogenic substrate N-methyl-N-p-toluenesulfonyl-L-lysine beta-naphthyl ester to screen colonies growing on agar for the presence of the enzyme. All of the mutations isolated map at locus tlp (typsin-like protease) which is cotransducible (approximately 1%) using phage P1 with tre (trehalose utilization) at approximately 58 min on the Salmonella map. Double mutants lacking both protease I and protease II have been constructed. These strains grew normally. They were able to degrade abnormal proteins and to carry out protein turnover during carbon starvation at the same rate as the wild type.
已分离出缺乏蛋白酶II(一种具有胰蛋白酶样特异性的内切蛋白酶)的鼠伤寒沙门氏菌突变体。这些突变体可以通过使用生色底物N-甲基-N-对甲苯磺酰-L-赖氨酸β-萘酯来筛选在琼脂上生长的菌落中该酶的存在来鉴定。所有分离出的突变都定位在tlp(胰蛋白酶样蛋白酶)位点,该位点在沙门氏菌图谱上约58分钟处,使用噬菌体P1与tre(海藻糖利用)共转导(约1%)。构建了同时缺乏蛋白酶I和蛋白酶II的双突变体。这些菌株生长正常。它们能够降解异常蛋白质,并在碳饥饿期间以与野生型相同的速率进行蛋白质周转。