PMID: 7029533Sep 1, 1981Paper

Role for membrane potential in the secretion of protein into the periplasm of Escherichia coli

Proceedings of the National Academy of Sciences of the United States of America
C J DanielsD L Oxender

Abstract

The leucine-specific binding protein of Escherichia coli is a periplasmic protein that is synthesized as a precursor and subsequently is processed during its secretion into the periplasmic space. The processing of both the leucine-specific binding protein and a plasmid-coded beta-lactamase is inhibited by phenethyl alcohol and by the proton ionophore, carbonylcyanide m-chlorophenylhydrazone (CCCP). The levels of CCCP that inhibit processing also produce significant decreases in the membrane potential. Valinomycin, a potassium ionophore, also inhibits processing of the leucine-specific binding protein in spheroplasts. Processing can be restored in CCCP-treated cells and in valinomycin-treated spheroplasts by dilution of the treated cells in fresh medium. These results suggest a role for membrane potential in the secretion of periplasmic proteins. A model is presented which suggests that membrane potential plays a primary role in the proper orientation of the precursor signal sequence within the membrane, thus promoting processing and secretion.

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Citations

Aug 1, 1991·Journal of Cellular Biochemistry·M D Adams, D L Oxender
Jun 1, 1994·Journal of Cellular Biochemistry·S L RuschD A Kendall
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