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J. Biol. Chem., Vol. 265, Issue 14, 8164-8169, 05, 1990
M Akita, S Sasaki, S Matsuyama and S Mizushima
SecA is an acidic, peripheral membrane protein involved in the
translocation of secretory proteins across the cytoplasmic membrane. The
direct interaction of SecA with secretory proteins was demonstrated by
means of chemical cross-linking with 1-ethyl-3-(3-
dimethylaminoprophyl)carbodiimide. OmpF-Lpp, a model secretory protein,
carries either an uncleavable or cleavable signal peptide, and mutant
secretory proteins derived from uncleavable OmpF-Lpp were used as
translocation substrates. The interaction was SecA-specific. None of the
control proteins, which are as acidic as SecA, was cross-linked with
uncleavable OmpF-Lpp. The interaction was signal peptide- dependent. The
interaction was increasingly enhanced as the number of positively charged
amino acid residues at the amino-terminal region of the signal peptide was
increased, irrespective of the species of amino acid residues donating the
charge. Finally, parallelism was observed between the efficiency of
interaction and that of translocation among mutant secretory proteins. It
is suggested that precursors of secretory proteins interact with SecA to
initiate the translocation reaction.
SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli
Institute of Applied Microbiology, University of Tokyo, Japan.
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