Interaction of cytoplasmic membrane and ribosomes in Escherichia coli: spectinomycin-induced disappearance of membrane protein I-19

Abstract

Incubation ofEscherichia 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.

Cytoplasmic membrane proteins of spectinomycin-susceptible and -resistant strains of Neisseria gonorrhoeae

“…The results of this study provide, for the first time in N. gonorrhoeae, direct evidence of altered cytoplasmic membrane composition in antibiotic-susceptible versus -resistant strains. The findings of this paper are similar to those for Escherichia coli noted by Mizuno et al (18). Two types of spectinomycin-resistant mutants were reported by these authors which differed in cytoplasmic membrane protein composition and phenotypic properties.…”

“…Ribosomes have been shown to be resistant to antibiotic action in other laboratory-derived Spcr mutants. This suggested that the action of spectinomycin was on the ribosomes and not directly on the cytoplasmic membrane (18).…”

Influence of sublethal concentrations of antibiotics on the expression of the mannose-specific ligand of Escherichia coli

“…Subinhibitory concentrations ofvarious antibiotics have been shown to cause differential inhibition or enhancement of various surface components of bacteria. Streptomycin and neomycin increase phospholipid in Serratia (2); kasugamycin, puromycin, and rifampin inhibit cytoplasmic proteins, whereas tetracycline and sparsomycin inhibit outer envelope proteins in E. coli (8); spectinomycin alone induces disappearance of membrane protein I-19 in E. coli (12). Other studies have shown that antibiotics induce changes in surface morphology (10), increase the organism's sensitivity to the bacteri-cidal action of serum (20), or interfere with genetic transfer than may involve surface components: chloramphenicol reduces gonococcal competence for transformation (3) and clindamycin inhibits conjugal transfer between E. coli strains (5).…”

Deletion mapping and heterogenote analysis of a mutation responsible for osmosis-sensitive growth, spectinomycin resistance, and alteration of cytoplasmic membrane in Escherichia coli

“…Based on these observations, Sucd Spcr mutants seem to be useful for elucidating genetically the nature of the interaction between ribosomes and the cytoplasmic membrane in bacterial cells as proposed by Mizuno et al (10). The pleiotropic effects of spectinomycin resistance mutation, such as the effect on the assembly of the 50S subunit as well as the 30S subunit of ribosomes (11) and on the stability of F plasmids (14,15), might be explained by altered interaction between ribosomes and the cytoplasmic membrane.…”