PT  - JOURNAL ARTICLE
AU  - Marcel Lagedroste
AU  - Jens Reiners
AU  - Sander H.J. Smits
AU  - Lutz Schmitt
TI  - Mechanism of the secretion of the lanthipeptide nisin
AID  - 10.1101/839423
DP  - 2019 Jan 01
TA  - bioRxiv
PG  - 839423
4099  - http://biorxiv.org/content/early/2019/11/12/839423.short
4100  - http://biorxiv.org/content/early/2019/11/12/839423.full
AB  - Lanthipeptides are ribosomally synthesized and post-translationally modified peptides containing dehydrated amino acids and (methyl-)lanthionine rings. One of the best-studied example is nisin, which is synthesized as a precursor peptide comprising of an N-terminal leader peptide and a C-terminal core peptide. Amongst others, the leader peptide is crucial for enzyme recognition and acts as a secretion signal for the ABC transporter NisT which secrets nisin in a proposed channeling mechanism. Here, we present an in vivo secretion analysis of this process in the presence and absence of the maturation machinery composed of the dehydratase NisB and the cyclase NisC. The data clearly demonstrated that the function of NisC, but the mere presence of NisB modulated the apparent secretion rates. Additional in vitro studies of detergent-solubilized NisT revealed how the activity of this ABC transporter is again influenced by the enzymes of the maturation machinery, but not the substrate.