Interaction of cytoplasmic membrane and ribosomes in Escherichia coli: spectinomycin-induced disappearance of membrane protein I-19.
AUTOR(ES)
Mizuno, T
RESUMO
Incubation of Escherichia coli with spectinomycin caused the disappearance of a major protein from the cytoplasmic membrane. This protein, called "I-19", was not a ribosomal protein. Its disappearance was not a result of the direct action of spectinomycin on the cytoplasmic membrane, but a result of its action on ribosomes. The disappearance was specifically induced by spectinomycin, and other antibiotics such as neomycin, erythromycin, and chloramphenicol had no effect. Although growth was not required for spectinomycin-induced disappearance of protein I-19 from the cytoplasmic membrane, the disappearance was not observed under conditions where protein synthesis was inhibited completely either by the addition of chloramphenicol or by cooling in ice. It is suggested that at least some ribosomes interact with the cytoplasmic membrane and that a modification of the mode of interaction through the action of spectinomycin on ribosomes caused the deletion of membrane protein I-19.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=234930Documentos Relacionados
- Coordinated alterations in ribosomes and cytoplasmic membrane in sucrose-dependent, spectinomycin-resistant mutants of Escherichia coli.
- Interaction between two major outer membrane proteins of Escherichia coli: the matrix protein and the lipoprotein.
- Interaction of Escherichia coli ribosomal protein S1 with ribosomes.
- Functional lac carrier protein in cytoplasmic membrane vesicles isolated from Escherichia coli: Temperature and pH dependence of dansyl-galactoside binding*
- A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli.