PMID:8436228

Citation	Nilsson, IM, Gafvelin, G and von Heijne, G (1993) Different sec-requirements for signal peptide cleavage and protein translocation in a model E. coli protein. FEBS Lett. 318:7-10
Abstract	We describe a secretory E. coli protein with a novel phenotype: signal peptide cleavage is largely unaffected whereas chain translocation is efficiently blocked under conditions where SecA, a central component of the secretory machinery, is rendered non-functional, and we have traced this phenotype to the presence of a mildly hydrophobic segment located approximately 30 residues downstream of the signal peptide. When this segment is deleted, normal SecA-dependent signal peptide cleavage and chain translocation is observed; when its hydrophobicity is increased, it becomes a permanent membrane anchor with cleavage of the signal peptide and membrane insertion both being SecA-independent. These findings suggest that the initial insertion of the signal peptide across the membrane can be uncoupled from the translocation process proper.
Links	PubMed
Keywords	Amino Acid Sequence; Bacterial Proteins/metabolism; Biological Transport; Cell Membrane/metabolism; Endopeptidases/chemistry; Endopeptidases/metabolism; Escherichia coli/metabolism; Membrane Proteins; Molecular Sequence Data; Protein Sorting Signals/metabolism; Serine Endopeptidases
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