| Literature DB >> 387716 |
Y S Cheng, D Zipser, C Y Cheng, S J Rolseth.
Abstract
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.Entities:
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Year: 1979 PMID: 387716 PMCID: PMC216787 DOI: 10.1128/jb.140.1.125-130.1979
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490