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Signal peptide mutants ofEscherichia coli

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Abstract

Numerous secretory proteins of the Gram-negative bacteriaE. coli are synthesized as precursor proteins which require an amino terminal extension known as the signal peptide for translocation across the cytoplasmic membrane. Following translocation, the signal peptide is proteolytically cleaved from the precursor to produce the mature exported protein. Signal peptides do not exhibit sequence homology, but invariably share common structural features: (1) The basic amino acid residues positioned at the amino terminus of the signal peptide are probably involved in precursor protein binding to the cytoplasmic membrane surface. (2) A stretch of 10 to 15 nonpolar amino acid residues form a hydrophobic core in the signal peptide which can insert into the lipid bilayer. (3) Small residues capable of β-turn formation are located at the cleavage site in the carboxyl terminus of the signal peptide. (4) Charge characteristics of the amino terminal region of the mature protein can also influence precursor protein export. A variety of mutations in each of the structurally distinct regions of the signal peptide have been constructedvia site-directed mutagenesis or isolated through genetic selection. These mutants have shed considerable light on the structure and function of the signal peptide and are reviewed here.

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Authors and Affiliations

  1. Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, 08854, Piscataway, New Jersey

    Joseph Gennity, Joel Goldstein & Masayori Inouye

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  1. Joseph Gennity
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  2. Joel Goldstein
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  3. Masayori Inouye
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Gennity, J., Goldstein, J. & Inouye, M. Signal peptide mutants ofEscherichia coli . J Bioenerg Biomembr 22, 233–269 (1990). https://doi.org/10.1007/BF00763167

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