Isolation and Characterization of Mutations in the Structural Gene for Protease III (ptr)
Overview
Authors
Affiliations
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.
Strategies to Enhance Periplasmic Recombinant Protein Production Yields in .
Karyolaimos A, Gier J Front Bioeng Biotechnol. 2021; 9:797334.
PMID: 34970535 PMC: 8712718. DOI: 10.3389/fbioe.2021.797334.
A common genetic system for functional studies of pitrilysin and related M16A proteases.
Alper B, Nienow T, Schmidt W Biochem J. 2006; 398(1):145-52.
PMID: 16722821 PMC: 1525005. DOI: 10.1042/BJ20060311.
Hydrolysis of Ribulose-1,5-bisphosphate Carboxylase by Endoproteinases from Senescing Barley Leaves.
Miller B, Huffaker R Plant Physiol. 1982; 69(1):58-62.
PMID: 16662184 PMC: 426145. DOI: 10.1104/pp.69.1.58.
Linkage map of Escherichia coli K-12, edition 10: the traditional map.
Berlyn M Microbiol Mol Biol Rev. 1998; 62(3):814-984.
PMID: 9729611 PMC: 98936. DOI: 10.1128/MMBR.62.3.814-984.1998.
Subcellular distribution of various proteases in Escherichia coli.
Swamy K, GOLDBERG A J Bacteriol. 1982; 149(3):1027-33.
PMID: 7037737 PMC: 216492. DOI: 10.1128/jb.149.3.1027-1033.1982.