Sec-mediated transport of posttranslationally dehydrated peptides in Lactococcus lactis
Article Abstract:
A study shows that the dehydration and cyclization of the nisin propeptide still occur when the nisin leader is preceded by the Sec signal peptide of Usp45 and that Sec system of Lactococcus lactis efficiently secretes dehydrated therapeutic peptides. The results have shown that besides the traditional lantibiotic transporter NisT, the Sec pathway with an established broad substrate range can be used for the improved export of lantibiotic enzyme-modified (poly)peptides.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2006
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Sec-mediated secretion of bacteriocin enterocin P by Lactococcus lactis
Article Abstract:
An investigation on the mechanism of secretion of the heterologously produced enterococcal bacteriocin P (EntP) His in Lactococcus lactis is conducted. EntP belongs to the class II bacteriocins that are synthesized as precursors with an N-terminal extension that demonstrated the typical tripartite structure of Sec-dependent signal peptides.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2005
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Dissection and modulation of the four distinct activities of nisin by mutagenesis of rings A and B by C-terminal truncation
Article Abstract:
The examination of the structural requirements and relevance of the N-terminal thioether rings of nisin by randomization of the ring A and B positions is presented. It could be engineered independently and give a basis for the design and synthesis of tailor-made analogs with desired activities.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2007
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