PMID:7565085
| Citation |
Håvarstein, LS, Diep, DB and Nes, IF (1995) A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates concomitant with export. Mol. Microbiol. 16:229-40 |
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| Abstract |
Lantibiotic and non-lantibiotic bacteriocins are synthesized as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 and -2. The double-glycine-type leader peptides are unrelated to the N-terminal signal sequences which direct proteins across the cytoplasmic membrane via the sec pathway. Their processing sites are also different from typical signal peptidase cleavage sites, suggesting that a different processing enzyme is involved. Peptide bacteriocins are exported across the cytoplasmic membrane by a dedicated ATP-binding cassette (ABC) transporter. Here we show that the ABC transporter is the maturation protease and that its proteolytic domain resides in the N-terminal part of the protein. This result demonstrates that the ABC transporter has a dual function: (i) removal of the leader peptide from its substrate, and (ii) translocation of its substrate across the cytoplasmic membrane. This represents a novel strategy for secretion of bacterial proteins. |
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| Keywords |
ATP-Binding Cassette Transporters/genetics; ATP-Binding Cassette Transporters/metabolism; Amino Acid Sequence; Bacteriocins/biosynthesis; Bacteriocins/genetics; Bacteriocins/metabolism; Base Sequence; Biological Transport; Conserved Sequence; Escherichia coli/metabolism; Genes, Bacterial; Molecular Sequence Data; Point Mutation; Protein Precursors/biosynthesis; Protein Precursors/genetics; Protein Sorting Signals/metabolism; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity; Transcriptional Activation |
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