Abstract
Protein export by bacteria has been widely studied in Escherichia coli and in Bacillus species. The mechanism of protein translocation across the cytoplasmic membrane of these organisms appears to be comparable to the translocation of proteins across the membrane of the rough endoplasmic reticulum of eukaryotic cells, and is described in several reviews (Michaelis and Beckwith 1982; Silhavy et al. 1983; Randall and Hardy 1984; Pugsley and Schwartz 1985). In gram-positive bacteria the exported proteins either remain anchored in the bacterial cell envelope, like the lipoproteins, or are released from the cells, like various proteases, amylase, and other proteins. In gram-negative bacteria the exported proteins are released into the periplasm, or are incorporated in the outer membrane of these cells. Apparently, the outer membrane of these organisms, which is both functionally and structurally completely different from the cytoplasmic membrane, forms an extra barrier for protein excretion into the extracellular space. Several gram-negative bacterial species, however, have been found to release extracellular proteins (Pugsley and Schwartz 1985), but very little is known about the mechnisms by which proteins are translocated across the outer membrane and about the possible role of signal or other topogenic sequences in this process.
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De Graaf, F.K., Oudega, B. (1986). Production and Release of Cloacin DF13 and Related Colicins. In: Wu, H.C., Tai, P.C. (eds) Protein Secretion and Export in Bacteria. Current Topics in Microbiology and Immunology, vol 125. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71251-7_11
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