Mutations in a new gene, secB, cause defective protein localization in Escherichia coli.
We isolated a new class of Escherichia coli mutants with pleiotropic defects in protein secretion. Using a previously described selection procedure (Oliver et al., Ann. Microbiol. [Paris] 133A:105-110, 1982), we obtained a large collection of strains containing mutations that affect protein localization. In many cases, the lesions causing the secretion defects were mapped in or near the previously identified gene, secA (Oliver and Beckwith, Cell 25:765-772, 1981). However, the selection also yielded mutants with mutations in a new locus, which was designated secB. These secB mutants were defective in the localization of maltose-binding protein and, in at least one case, OmpF protein. Double mutants with lesions in both secA and secB had strong defects in the secretion of maltose-binding protein and OmpF protein. The secB locus mapped near cysE at min 80.5 on the E. coli genetic map. The properties of secB mutants suggest that the secB product could be a component of the E. coli secretory apparatus.
D001426:Bacterial Proteins / Q000235:genetics*; D002874:Chromosome Mapping; D002876:Chromosomes, Bacterial; D004926:Escherichia coli / Q000235:genetics*; D005798:Genes, Bacterial; D009154:Mutation; D001616:beta-Galactosidase / Q000235:genetics
D001426:Bacterial Proteins; D001616:beta-Galactosidase