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. 2011 Mar 2;133(8):2338-41.
doi: 10.1021/ja109044r. Epub 2010 Nov 29.

Production of lantipeptides in Escherichia coli

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Free PMC article

Production of lantipeptides in Escherichia coli

Yanxiang Shi et al. J Am Chem Soc. .
Free PMC article

Abstract

Lantipeptides are ribosomally synthesized and posttranslationally modified peptides containing thioether cross-links. We describe the preparation of seven different lantipeptides in Escherichia coli and demonstrate that this methodology can be used to incorporate nonproteinogenic amino acids.

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Figures

Figure 1
Figure 1
Posttranslational modifications in lantipeptide biosynthesis. Dha, dehydrolalanine; Dhb, dehydrobutyrine; Abu, 2-aminobutyric acid.
Figure 2
Figure 2
(A) Sequences of the ProcA lantipeptide core peptides used in this study. The residue replaced by pBpa in this work is highlighted in red. For the sequences of the leader peptides, see Figure S1. (B) Representative structures of prochlorosins 1.7 and 3.3. Abu, 2-aminobutyric acid; Dha, dehydroalanine; Dhb, dehydrobutyrine.
Figure 3
Figure 3
MALDI-MS spectra of precursor peptides modified by ProcM in E. coli and treated with a protease to remove the leader peptide. (A) ProcA1.7, (B) ProcA2.11, (C) ProcA3.3, and (D) ProcA3.2 Phe26pBpa.
Figure 4
Figure 4
(A) Sequences of the HalA core peptides. For the sequences of the leader peptides, see Figure S1. (B) Structures of haloduracin α and β. Abu, 2-aminobutyric acid; Dha, dehydroalanine; Dhb, dehydrobutyrine.
Figure 5
Figure 5
MALDI-MS spectra of precursor peptides modified in E. coli and treated with a protease to remove the leader peptide. (A) HalA1, (B) HalA2, and (C) NisA.
Figure 6
Figure 6
Antimicrobial assays against L. lactis HP. (1) authentic nisin; (2) nisin produced in E. coli; (3) Halα produced in E. coli combined with authentic Halβ; (4) authentic Halα combined with Halβ produced in E. coli; (5) authentic Halα and Halβ; (6) Halα and Halβ both produced in E. coli.

References

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