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Recent advances in the biosynthesis of RiPPs from multicore-containing precursor peptides.

ABSTRACT: Ribosomally synthesized and post-translationally modified peptides (RiPPs) compose a large structurally and functionally diverse family of natural products. The biosynthesis system of RiPPs typically involves a precursor peptide comprising of a leader and core motif and nearby processing enzymes that recognize the leader and act on the core for producing modified peptides. Interest in RiPPs has increased substantially in recent years as improvements in genome mining techniques have dramatically improved access to these peptides and biochemical and engineering studies have supported their applications. A less understood, intriguing feature in the RiPPs biosynthesis is the precursor peptides of multiple RiPPs families produced by bacteria, fungi and plants carrying multiple core motifs, which we term "multicore". Herein, we present the prevalence of the multicore systems, their biosynthesis and engineering for applications.

SUBMITTER: Rubin GM

PROVIDER: S-EPMC7666021 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

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Recent advances in the biosynthesis of RiPPs from multicore-containing precursor peptides.

Rubin Garret M GM Ding Yousong Y

Journal of industrial microbiology & biotechnology 20200702 9-10

Ribosomally synthesized and post-translationally modified peptides (RiPPs) compose a large structurally and functionally diverse family of natural products. The biosynthesis system of RiPPs typically involves a precursor peptide comprising of a leader and core motif and nearby processing enzymes that recognize the leader and act on the core for producing modified peptides. Interest in RiPPs has increased substantially in recent years as improvements in genome mining techniques have dramatically ...[more]

PMID: 32617877

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