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Effects of inhibitors of membrane signal peptide peptidase on protein translocation into membrane vesicles

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Abstract

The effect of the removal of signal peptides after cleavage of precursor molecules by the signal peptidase I was examined in an in vitro translocation system with Escherichia coli membrane vesicles. The translocation of periplasmic alkaline phosphatase precursors was significantly inhibited by the protease inhibitors antipain, elastatinal and leupeptin. Antipain and leupeptin enhanced the translocation of precursors of outer membrane protein OmpA, but inhibited the processing. However, antipain did not inhibit the processing of precursors mediated by signal peptidase I in the soluble form. Moreover, the inhibition by antipain was not due to the disruption of membrane integrity, but occurred during the process of protein translocation. Since these small peptide inhibitors are known to inhibit membrane protease IV, a signal peptide peptidase, these results suggest that the hydrolysis of signal peptides is an important step in the recycles of the overall translocation process, and that the prevention of degradation of signal peptides feedback inhibits the preceding steps in the translocation pathway.

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Authors and Affiliations

  1. Department of Fine Structure, Boston Biomedical Research Institute, 02114, Boston, MA, USA

    Lingling Chen & Phang C. Tai

  2. Department of Microbiology and Molecular Genetics, Harvard Medical School, 02115, Boston, MA, USA

    Lingling Chen & Phang C. Tai

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  1. Lingling Chen
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  2. Phang C. Tai
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Dedicated to John L. Ingraham on the occasion of his “retirement”; his approaches and enthusiasm for science remain an inspiration to PCT, who has been guided by his motto, “Science should be fun,” for the last twenty years

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Chen, L., Tai, P.C. Effects of inhibitors of membrane signal peptide peptidase on protein translocation into membrane vesicles. Arch. Microbiol. 153, 90–94 (1989). https://doi.org/10.1007/BF00277547

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  • DOI: https://doi.org/10.1007/BF00277547

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