The chemistry and enzymology of the type I signal peptidases

Authors

  • Ross E. Dalbey,

    1. Department of Chemistry, The Ohio State University, 120 West 18th Avenue, Columbus, Ohio, 43210
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  • Mark O. Lively,

    Corresponding author
    1. Biochemistry Department, Bowman Gray School of Medicine, Wake Forest University, Medical Center Blvd., Winston-Salem, North Carolina 27157
    • Department of Biochemistry, Bowman Gray School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157

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  • Sierd Bron,

    1. Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, Kerklaan 30, 9751 NN, Haren (GN), The Netherlands
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  • Jan Maarten Van Dijl

    1. Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, Kerklaan 30, 9751 NN, Haren (GN), The Netherlands
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Abstract

The discovery that proteins exported from the cytoplasm are typically synthesized as larger precursors with cleavable signal peptides has focused interest on the peptidases that remove the signal peptides. Here, we review the membrane-bound peptidases dedicated to the processing of protein precursors that are found in the plasma membrane of prokaryotes and the endoplasmic reticulum, the mitochondrial inner membrane, and the chloroplast thylakoidal membrane of eukaryotes. These peptidases are termed type I signal (or leader) peptidases. They share the unusual feature of being resistant to the general inhibitors of the four well-characterized peptidase classes. The eukaryotic and prokaryotic signal peptidases appear to belong to a single peptidase family. This review emphasizes the evolutionary concepts, current knowledge of the catalytic mechanism, and substrate specificity requirements of the signal peptidases.

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