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The assembly of the major outer membrane protein OmpF of Escherichia coli depends on lipid synthesis.

1988; Springer Nature; Volume: 7; Issue: 11 Linguagem: Inglês

10.1002/j.1460-2075.1988.tb03237.x

1460-2075

Jean‐Michel Bolla, Claude Lazdunski, Jean‐Marie Pagès,

RNA and protein synthesis mechanisms

Research Article1 November 1988free access The assembly of the major outer membrane protein OmpF of Escherichia coli depends on lipid synthesis. J. M. Bolla J. M. Bolla Centre de Biochimie et de Biologie Moléculaire, CNRS, Marseille, France. Search for more papers by this author C. Lazdunski C. Lazdunski Centre de Biochimie et de Biologie Moléculaire, CNRS, Marseille, France. Search for more papers by this author J. M. Pagès J. M. Pagès Centre de Biochimie et de Biologie Moléculaire, CNRS, Marseille, France. Search for more papers by this author J. M. Bolla J. M. Bolla Centre de Biochimie et de Biologie Moléculaire, CNRS, Marseille, France. Search for more papers by this author C. Lazdunski C. Lazdunski Centre de Biochimie et de Biologie Moléculaire, CNRS, Marseille, France. Search for more papers by this author J. M. Pagès J. M. Pagès Centre de Biochimie et de Biologie Moléculaire, CNRS, Marseille, France. Search for more papers by this author Author Information J. M. Bolla1, C. Lazdunski1 and J. M. Pagès1 1Centre de Biochimie et de Biologie Moléculaire, CNRS, Marseille, France. The EMBO Journal (1988)7:3595-3599https://doi.org/10.1002/j.1460-2075.1988.tb03237.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Cerulenin, a drug which specifically blocks lipid synthesis, prevented both the trimerization of OmpF monomers and their assembly into the outer membrane of Escherichia coli B cells. A monoclonal antibody directed against a surface-exposed epitope of the trimer was used to probe the assembly of OmpF in the presence or absence of the drug. An inhibition level of 80% was reached 16 min after the addition of cerulenin. The accumulated monomeric form could not be assembled even after lipid synthesis was restored. Instead, it was slowly degraded. It was further shown that the inhibition of assembly resulted in a rapid inhibition of OmpF synthesis. These data demonstrate that there is a direct relationship between the synthesis of lipid (most likely lipopolysaccharide) and the correct export of OmpF. This coupling is required to promote the trimerization of the porin monomer and its assembly into the outer membrane. Previous ArticleNext Article Volume 7Issue 111 November 1988In this issue RelatedDetailsLoading ...