Sec-mediated secretion of bacteriocin enterocin P by Lactococcus lactis.
Most lactic acid bacterium bacteriocins utilize specific leader peptides and dedicated machineries for secretion. In contrast, the enterococcal bacteriocin enterocin P (EntP) contains a typical signal peptide that directs its secretion when heterologously expressed in Lactococcus lactis. Signal peptide mutations and the SecA inhibitor azide blocked secretion. These observations demonstrate that EntP is secreted by the Sec translocase.
Herranz
Carmen
C
Department of Microbiology, Groningen Biomolecualr Sciences and Biotechnology Institute, University of Groningen, Haren, The Netherlands.
Driessen
Arnold J M
AJ
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001430:Bacteriocins / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D016984:Enterococcus faecium / Q000187:drug effects / Q000235:genetics / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D013294:Lactococcus lactis / Q000235:genetics / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008826:Microbial Sensitivity Tests; D021382:Protein Sorting Signals / Q000235:genetics*; D000069816:SEC Translocation Channels; D000081416:SecA Proteins
D001426:Bacterial Proteins; D001430:Bacteriocins; D026901:Membrane Transport Proteins; D021382:Protein Sorting Signals; D000069816:SEC Translocation Channels; C417717:enterocin P; D000251:Adenosine Triphosphatases; D000081416:SecA Proteins