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Activation of a Cryptic Gene Cluster in Lysobacter enzymogenes Reveals a Module/Domain Portable Mechanism of Nonribosomal Peptide Synthetases in the Biosynthesis of Pyrrolopyrazines

Author:
Li, Shanren, Wu, Xiuli, Zhang, Limei, Shen, Yuemao, Du, Liangcheng
Source:
Organic letters 2017 v.19 no.19 pp. 5010-5013
ISSN:
1523-7052
Subject:
Lysobacter enzymogenes, biosynthesis, chemical reactions, chemical structure, gene silencing, ligases, multigene family, organic compounds
Abstract:
Lysobacter are considered “peptide specialists”. However, many of the nonribosomal peptide synthetase genes are silent. Three new compounds were identified from L. enzymogenes upon activating the six-module-containing led cluster by the strong promoter PHSAF. Although ledD was the first gene under PHSAF control, the second gene ledE was expressed the highest. Targeted gene inactivation showed that the two-module LedE and the one-module LedF were selectively used in pyrrolopyrazine biosynthesis, revealing a module/domain portable mechanism.
Agid:
5826914