期刊
FEBS JOURNAL
卷 288, 期 14, 页码 4348-4363出版社
WILEY
DOI: 10.1111/febs.15724
关键词
ABC transporter; antimicrobial peptides; lanthipeptide; leader peptide; peptide secretion
资金
- Deutsche Forschungsgemeinschaft (DFG) [Schm1279/31-1]
Lanthipeptides are ribosomally synthesized and posttranslationally modified peptides, consisting of a leader peptide and a core peptide. The leader peptide is essential for enzyme recognition and secretion, while the core peptide is the target site for posttranslational modifications. Studying model lanthipeptides like nisin provides insights into their modification and secretion processes.
Lanthipeptides are ribosomally synthesized and posttranslationally modified peptides. Their precursor peptide comprises of an N-terminal leader peptide and a C-terminal core peptide. Here, the leader peptide is crucial for enzyme recognition especially for the modification enzymes and acts furthermore as a secretion signal for the lanthipeptide exporter. The core peptide is the target site for the posttranslational modifications and contains dehydrated amino acids and lanthionine rings. Nisin produced by the Gram-positive bacterium Lactococcus lactis is one of the best-studied lanthipeptides and used as a model system to study their modification and secretion processes. Nisin is secreted as a precursor peptide. Here, we present an in vivo secretion analysis of NisT in the absence of the modification machinery allowing the secretion of leader peptide mutants and their impact solely on the secretion activity of NisT. Additionally, we created leader peptide hybrids to provide new insights, how the secretion is effected by unnatural leader peptides. The focus on the secretion activity of the transporter alone enabled us to determine the recognition site of NisT within the leader peptide of nisin.
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