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. 2020 May 8;11:2272. doi: 10.1038/s41467-020-16145-4

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a Chemical structure of lactazole A. b Comparison of laz BGC with other prototypical thiopeptide BGCs. Homologs of laz genes are color-coded. Genes encoding enzymes responsible for the installation of azolines, azoles, dehydroalanine, and pyridine are shown in light blue, blue, green, and orange, respectively. Precursor peptide structural genes are shown in black and ancillary genes absent from laz BGC are in white. c Comparison of primary sequences for thiopeptides from b, with the same PTM color coding. The comparison reveals an unusual macrocycle size, low C/S/T content, and the absence of azole modification in position 2 as unique features of lactazole. d Summary of the FIT-Laz system and the roles of individual enzymes during lactazole biosynthesis. In FIT-Laz, synthetic DNA templates encoding LazA or its mutants are in-vitro transcribed and translated to generate precursor peptides, which undergo a cascade of PTMs introduced by lactazole biosynthetic enzymes to yield lactazole A or its artificial analogs.