2018
DOI: 10.1039/c7cc08620b
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Albusnodin: an acetylated lasso peptide fromStreptomyces albus

Abstract: We describe a lasso peptide, albusnodin, that is post-translationally modified with an acetyl group, the first example of a lasso peptide with this modification. Using heterologous expression, we further show that the acetyltransferase colocalized with the albusnodin gene cluster is required for the biosynthesis of this lasso peptide. This type of lasso peptide is widespread in Actinobacteria with 44 examples found in currently sequenced genomes.

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Cited by 52 publications
(59 citation statements)
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“…Moreover, lasso peptides, which belong to the ribosomally synthesized and posttranslationally modified peptide (RiPP) family of natural products, are encoded in relatively small BGCs, facilitating DNA synthesis. Most importantly, lasso peptides have attracted significant attention due to their thermal 12 and proteolytic 13 stability, diverse biological activities, 14 and susceptibility to structural modification such as epitope grafting 15,16 and DNA-encoded compound libraries. 17 Lasso peptides are characterized by a distinctive lariat knot-like topology or 1-rotaxane structure.…”
mentioning
confidence: 99%
“…Moreover, lasso peptides, which belong to the ribosomally synthesized and posttranslationally modified peptide (RiPP) family of natural products, are encoded in relatively small BGCs, facilitating DNA synthesis. Most importantly, lasso peptides have attracted significant attention due to their thermal 12 and proteolytic 13 stability, diverse biological activities, 14 and susceptibility to structural modification such as epitope grafting 15,16 and DNA-encoded compound libraries. 17 Lasso peptides are characterized by a distinctive lariat knot-like topology or 1-rotaxane structure.…”
mentioning
confidence: 99%
“…In Bacillus pseudomycoides DSM 12442, producer of pseudomycoidin, the presence of the PsmN, a nucleotidyltransferase, was associated with the glycosylation of the C-terminal region (Zyubko et al, 2019). The advantages that these chemical modifications offer to the lasso peptides remains unclear, but they may affect peptide stability (Zyubko et al, 2019), regulate critical processes, such as signaling pathways (Zhu et al, 2016b) or influence the functioning of self-immunity systems in the producer cells (Zhu et al, 2016c;Zong et al, 2018). A gene encoding a protein belonging to the PqqD enzyme superfamily frequently co-occurred with the lasso peptide biosynthesis genes in species of the genera Butyrivibrio and Lachnospira.…”
Section: Discussionmentioning
confidence: 99%
“…The heterologous expression of acetylated lasso peptides also required a Streptomyces host. Lasso peptide, albusnodin, encoded in the genome of S albus DSM 41398 is heterologously expressed in the hosts Streptomyces coelicolor and S. lividans (Zong et al, 2018). Sviceucin originating from Streptomyces sviceus is heterologously produced in good yield (15 mg/L of culture) in S. coelicolor (Li et al, 2015).…”
Section: Heterologous Expression Of Lassomentioning
confidence: 99%