Deg phenotype of Escherichia coli lon mutants.
AUTOR(ES)
Gottesman, S
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=222096Documentos Relacionados
- Proteolysis and modulation of the activity of the cell division inhibitor SulA in Escherichia coli lon mutants.
- Overexpression of Protease-Deficient DegPS210A Rescues the Lethal Phenotype of Escherichia coli OmpF Assembly Mutants in a degP Background
- Membrane cytochromes of Escherichia coli chl mutants.
- Escherichia coli recBC deletion mutants.
- Alp, a suppressor of lon protease mutants in Escherichia coli.
