Abstract
Humidimycin (MDN-0010) is a ribosomally synthesized and post-translationally modified peptide (RiPP) belonging to class I lasso peptides, and is structurally related to siamycins, which have been shown to have strong antimicrobial activities against Gram-positive bacteria and to possess anti-HIV activity. Humidimycin was isolated from the strain Streptomyces humidus CA-100629, and was shown to synergize the activity of the fungal cell wall inhibitor caspofungin. In this work, the biosynthetic gene cluster of humidimycin was identified by genome mining of S. humidus CA-100629, cloned by Gibson assembly, and heterologously expressed.
Highlights
Natural products are non-essential small molecules produced by plants, microbes, and invertebrates
Among ribosomally synthesized and post-translationally modified peptide (RiPP), lasso peptides are cyclic peptides, containing an N-terminal macrolactam ring comprised of seven to nine amino acid residues and a linear C-terminal peptide tail threaded through the ring
We present the identification, cloning, and heterologous expression of the demonstrate that the C-terminal tryptophan of humidimycin is epimerized in both wild-type and humidimycin biosynthetic gene clusters (BGCs) after genome mining of the producer strain S. humidus CA-100629
Summary
Natural products are non-essential small molecules produced by plants, microbes, and invertebrates. Inteam otheras a new synergist of thefor of an theisopeptidase fungal cell wall biosynthesis caspofungin (CAS) It has been dramatic increase in the number of cases of life-threatening fungal infections and the lack of effective proposed that clusters containing ABC-transporters might produce antimicrobial lasso peptides, while drugs make theisopeptidases developmentmight of novel approaches to fight against these infectious diseases those containing produce lasso peptides with another function [21]. Lasso peptides, it might be expected that other molecules of this group, including humidimycin, The BGCs of additional class I siamycin-like molecules (aborycin, specialicin, and MS-271) have inhibit peptidoglycan biosynthesis [27]. We present the identification, cloning, and heterologous expression of the demonstrate that the C-terminal tryptophan of humidimycin is epimerized in both wild-type and humidimycin BGC (hum) after genome mining of the producer strain S. humidus CA-100629.
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