title: Deg phenotype of Escherichia coli lon mutants.
abstract: Deg. one of the Escherichia coli systems for degrading abnormal polypeptides (e.g., nonsense fragments), is also involved in the degradation of some classes of missense proteins. Both missense proteins of beta-galactosidase and temperature-sensitive phage products appear to be degraded by the Deg system. Mutations in the Deg system are indistinguishable from mutations classically called lon or capR; all map near proC, all are mucoid, defective in protein degradation, sensitive to radiomimetic agents, and defective in P1 lysogenization. All are able to propagate temperature-sensitive phage better than lon+ parental strains. Mutations that suppress the radiation sensitivity of these strains (sul) also suppress the P1 lysogenization defect, but do not affect mucoidy or the degradation defect.
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D002874:Chromosome Mapping; D004926:Escherichia coli / Q000235:genetics*; D005696:Galactosidases / Q000378:metabolism*; D005838:Genotype; D006025:Glycosaminoglycans / Q000096:biosynthesis; D010641:Phenotype; D011135:Polysaccharides, Bacterial / Q000096:biosynthesis; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D006025:Glycosaminoglycans; D011135:Polysaccharides, Bacterial; D005696:Galactosidases