Mutations near the cleavage site of enterocin NKR-5-3B prepeptide reveal new insights into its biosynthesis

Rodney H. Perez, Haruki Sugino, Naoki Ishibashi, Takeshi Zendo, Pongtep Wilaipun, Vichien Leelawatcharamas, Jiro Nakayama, Kenji Sonomoto

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Enterocin NKR-5-3B (Ent53B) is a 64-residue novel circular bacteriocin synthesized from an 87-residue prepeptide. Albeit through a still unknown mechanism, the EnkB1234 biosynthetic enzyme complex processes the prepeptide to yield its mature active, circular form. To gain insights into the key region/residue that plays a role in Ent53 maturation, several mutations near the cleavage site on the precursor peptide were generated. The interaction of the precursor peptide and EnkB1234 appeared to be hydrophobic in nature. At the Leu1 position, only mutations with helix structure-promoting hydrophobic residues (Ala, Ile, Val or Phe) were able to yield the mature Ent53B derivative. In this study, we also highlight the possible conformation-stabilizing role of the Ent53B leader peptide on the precursor peptide for its interaction with its biosynthetic enzyme complex. Any truncations of the leader peptide moiety interfered in the processing of the prepeptide. However, when propeptides of other circular bacteriocins (circularin A, leucocyclicin Q or lactocyclicin Q) were cloned at the C-terminus of the leader peptide, EnkB1234 could not process them to yield a mature bacteriocin. Taken together, these findings offer new perspectives in our understanding of the possible molecular mechanism of the biosynthesis of this circular bacteriocin. These new perspectives will help advance our current understanding to eventually elucidate circular bacteriocin biosynthesis. Understanding the biosynthetic mechanism of circular bacteriocins will materialize their application potential.

Original languageEnglish
Article number000435
Pages (from-to)431-441
Number of pages11
JournalMicrobiology (United Kingdom)
Volume163
Issue number4
DOIs
Publication statusPublished - Apr 1 2017

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Bacteriocins
Mutation
Protein Sorting Signals
Peptides
Enzymes
enterocin

All Science Journal Classification (ASJC) codes

  • Microbiology

Cite this

Perez, R. H., Sugino, H., Ishibashi, N., Zendo, T., Wilaipun, P., Leelawatcharamas, V., ... Sonomoto, K. (2017). Mutations near the cleavage site of enterocin NKR-5-3B prepeptide reveal new insights into its biosynthesis. Microbiology (United Kingdom), 163(4), 431-441. [000435]. https://doi.org/10.1099/mic.0.000435

Mutations near the cleavage site of enterocin NKR-5-3B prepeptide reveal new insights into its biosynthesis. / Perez, Rodney H.; Sugino, Haruki; Ishibashi, Naoki; Zendo, Takeshi; Wilaipun, Pongtep; Leelawatcharamas, Vichien; Nakayama, Jiro; Sonomoto, Kenji.

In: Microbiology (United Kingdom), Vol. 163, No. 4, 000435, 01.04.2017, p. 431-441.

Research output: Contribution to journalArticle

Perez, RH, Sugino, H, Ishibashi, N, Zendo, T, Wilaipun, P, Leelawatcharamas, V, Nakayama, J & Sonomoto, K 2017, 'Mutations near the cleavage site of enterocin NKR-5-3B prepeptide reveal new insights into its biosynthesis', Microbiology (United Kingdom), vol. 163, no. 4, 000435, pp. 431-441. https://doi.org/10.1099/mic.0.000435
Perez, Rodney H. ; Sugino, Haruki ; Ishibashi, Naoki ; Zendo, Takeshi ; Wilaipun, Pongtep ; Leelawatcharamas, Vichien ; Nakayama, Jiro ; Sonomoto, Kenji. / Mutations near the cleavage site of enterocin NKR-5-3B prepeptide reveal new insights into its biosynthesis. In: Microbiology (United Kingdom). 2017 ; Vol. 163, No. 4. pp. 431-441.
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