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- W2533016775 abstract "Lasso peptides are a class of ribosomally synthesized and post-translationally modified peptides (RiPPs) with a unique lariat knot-like fold that endows them with extraordinary stability and biologically relevant activity. However, the biosynthetic mechanism of these fascinating molecules remains largely speculative. Generally, two enzymes (B for processing and C for cyclization) are required to assemble the unusual knot-like structure. Several subsets of lasso peptide gene clusters feature a split B protein on separate open reading frames (B1 and B2), suggesting distinct functions for the B protein in lasso peptide biosynthesis. Herein, we provide new insights into the role of the RiPP recognition element (RRE) PadeB1, characterizing its capacity to bind the paeninodin leader peptide and deliver its peptide substrate to PadeB2 for processing." @default.
- W2533016775 created "2016-10-28" @default.
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- W2533016775 date "2016-10-18" @default.
- W2533016775 modified "2023-10-16" @default.
- W2533016775 title "The B1 Protein Guides the Biosynthesis of a Lasso Peptide" @default.
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- W2533016775 doi "https://doi.org/10.1038/srep35604" @default.
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