Cheng Y S, Zipser D, Cheng C Y, Rolseth S J
J Bacteriol. 1979 Oct;140(1):125-30. doi: 10.1128/jb.140.1.125-130.1979.
Escherichia coli mutants defective in protease III were isolated by enzyme assays of heavily mutagenized colones. One mutant produced thermolabile enzyme, and it is presumed to have a mutation in the structural gene of protease III. Two other mutants mapping at the same site had less than 5% of the wild-type protease III level. The genetic locus of these mutations, designated ptr, was located at approximately 60 min on the E. coli linkage map based on its high frequency (70%) of contransduction by P1 with argA. Strains with less than 5% of the wild-type protease III activity grew normally and degraded nonsense fragments of beta-galactosidase at wild-type rates.
通过对大量诱变菌落进行酶活性测定,分离出了蛋白酶III缺陷型的大肠杆菌突变体。其中一个突变体产生的酶对热不稳定,推测其蛋白酶III的结构基因发生了突变。另外两个位于同一位置的突变体,其蛋白酶III水平不到野生型的5%。这些突变的基因位点命名为ptr,基于其与argA被P1共转导的高频性(70%),位于大肠杆菌连锁图谱上大约60分钟处。蛋白酶III活性不到野生型5%的菌株生长正常,并以野生型速率降解β-半乳糖苷酶的无义片段。