Regulation of ompF porin expression by salicylate in Escherichia coli
نویسندگان
چکیده
منابع مشابه
Novel mechanism of Escherichia coli porin regulation.
A novel mechanism of Escherichia coli porin regulation was discovered from multicopy suppressors that permitted growth of cells expressing a mutant OmpC protein in the absence of DegP. Analyses of two suppressors showed that both substantially lowered OmpC expression. Suppression activities were confined to a short DNA sequence, which we designated ipeX for inhibition of porin expression, and t...
متن کاملTrimerization of an in vitro synthesized OmpF porin of Escherichia coli outer membrane.
The assembly of outer membrane proteins of Escherichia coli was examined using the OmpF porin as a model. Since this protein is made as a precursor, which is processed to a protein of Mr 37,000 before being assembled into trimers in the outer membrane, we synthesized a modified OmpF, which lacked 16 out of 22 amino acid residues from its signal sequence, in a coupled transcription-translation s...
متن کاملCloning and sequencing of ompf Salmonella typhi Salmonella ompf gene in Escherichia coli Origami
Background and Aim: Salmonella Typhi belongs to the family Enterobacteriaceae, gram-negative bacilli and causes gastrointestinal diseases such as typhoid. This bacterium has a special structure and various genes, including the ompf gene (outer membrane protein). Recent studies have shown the possibility of using ompf in the development of a diagnostic tuberculosis vaccine. Therefore, the aim of...
متن کاملLipopolysaccharide structure required for in vitro trimerization of Escherichia coli OmpF porin.
Deep rought mutants, which produce very defective lipopolysaccharides, are unable to export normal levels of porins into the outer membrane. In this study, we showed that lipopolysaccharides from such mutants were also unable to facilitate the trimerization, in vitro, of monomeric OmpF porin secreted by spheroplasts of Escherichia coli B/r. In contrast, lipopolysaccharides containing most or al...
متن کاملInteraction of aminoglycosides with the outer membranes and purified lipopolysaccharide and OmpF porin of Escherichia coli.
The mechanism of uptake of aminoglycosides across the outer membrane of Escherichia coli was reevaluated. Porin-deficient mutants showed no alteration in gentamicin or kanamycin susceptibility. Furthermore, the influence of kanamycin on intrinsic tryptophan fluorescence of porin OmpF (Y. Kobayashi, and T. Nakae, Eur. J. Biochem. 151:231-236, 1985) was shown to be strongly influenced by protein ...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1991
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.173.18.5631-5638.1991