Abstract
Most secreted proteins of both eukaryotes and prokaryotes are synthesized as preproteins with NH2-terminal hydrophobic signal sequences which are removed during transfer of the proteins across the membrane1,2. The role of cleavable signal sequences in the insertion of proteins into the cytoplasmic membrane is not clear. Rothman and Lenard have proposed that the assembly of those integral membrane proteins that have a substantial extracytoplasmic domain (ectoproteins) occurs by a similar mechanism to that of secreted proteins, involving a cleavable signal sequence, but with complete secretion being prevented by a hydrophobic COOH–terminal region3. In eukaryotes, several ectoproteins seem to be synthesized in this way4–6 but in prokaryotes, the coat protein of M13 phage is the only reported example of a cytoplasmic membrane protein that is made as a preprotein2,7, although a non-cleavable signal-like sequence has been shown for the E. coli lactose permease8. We show here that penicillin-binding proteins 5 and 6 of Escheri-chia coli are the first examples of cytoplasmic membrane proteins, encoded by bacteria, that are processed.
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Pratt, J., Holland, I. & Spratt, B. Precursor forms of penicillin-binding proteins 5 and 6 of E. coli cytoplasmic membrane. Nature 293, 307–309 (1981). https://doi.org/10.1038/293307a0
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DOI: https://doi.org/10.1038/293307a0
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