Characterization of the biosynthetic gene cluster of enterocin f4-9, a glycosylated bacteriocin

Mohamed Abdelfattah Maky, Naoki Ishibashi, Jiro Nakayama, Takeshi Zendo

研究成果: Contribution to journalArticle査読

1 被引用数 (Scopus)

抄録

Enterocin F4-9 belongs to the glycocin family having post-translational modifications by two molecules of N-acetylglucosamine β-O-linked to Ser37 and Thr46. In this study, the biosynthetic gene cluster of enterocin F4-9 was cloned and expressed in Enterococcus faecalis JH2-2. Production of glycocin by the JH2-2 expression strain was confirmed by expression of the five genes. The molecular weight was greater than glycocin secreted by the wild strain, E. faecalis F4-9, because eight amino acids from the N-terminal leader sequence remained attached. This N-terminal extension was eliminated after treatment with the culture supernatant of strain F4-9, implying an extracellular protease from E. faecalis F4-9 cleaves the N-terminal sequence. Thus, leader sequences cleavage requires two steps: the first via the EnfT protease domain and the second via extracellular proteases. Interestingly, the long peptide, with N-terminal extension, demonstrated advanced antimicrobial activity against Gram-positive and Gram-negative bacteria. Furthermore, enfC was responsible for glycosylation, a necessary step prior to secretion and cleavage of the leader peptide. In addition, enfI was found to grant self-immunity to producer cells against enterocin F4-9. This report demonstrates specifications of the minimal gene set responsible for production of enterocin F4-9, as well as a new biosynthetic mechanism of glycocins.

本文言語英語
論文番号2276
ジャーナルMicroorganisms
9
11
DOI
出版ステータス出版済み - 11 2021

All Science Journal Classification (ASJC) codes

  • 微生物学
  • 微生物学(医療)
  • ウイルス学

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