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Updated: May 22, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
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Published on: February 22, 2014

RiPP recognition elements evolved to prevent pathway interference through leader peptide discrimination.

Aleksandr Popov1,2, Dmitry Bikmetov3, Anastasiia Grigoreva3

  • 1RIKEN Center for Integrative Medical Sciences, Yokohama, Japan.

Nature Communications
|May 20, 2026
PubMed
Summary
This summary is machine-generated.

We discovered new ribosomally synthesized and post-translationally modified peptides (RiPPs) in Bacillota. These RiPPs evolved mechanisms to coexist with lasso peptides, revealing insights into natural product biosynthesis and evolution.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Natural Product Discovery

Background:

  • Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a diverse class of natural products.
  • RiPP biosynthesis often involves specific interactions between precursor peptides and adapter proteins like RiPP recognition elements (RREs).
  • The co-localization of RiPP and lasso peptide gene clusters in Bacillota suggests potential pathway conflicts.

Purpose of the Study:

  • To investigate a newly discovered family of RiPPs found in Bacillota genomes.
  • To understand the molecular mechanisms enabling the coexistence of distinct RiPP biosynthetic pathways, specifically RiPPs and lasso peptides.
  • To elucidate the evolutionary strategies employed by these systems to avoid pathway interference.

Main Methods:

  • Bioinformatic analysis of RiPP biosynthetic gene clusters in Bacillota.
  • Biochemical assays to study protein-peptide interactions.
  • Structural biology techniques to determine key molecular interactions.

Main Results:

  • Discovery of a widespread family of RiPPs in Bacillota, often co-localizing with lasso peptides.
  • Identification of conserved RRE-binding motifs on precursor peptides.
  • Biochemical and structural data revealing how cognate recognition and discrimination between precursor peptides and leader peptidases are achieved.
  • Demonstration of mechanisms allowing the coexistence of two RiPP biosynthetic systems within a single host.

Conclusions:

  • The discovered RiPP family possesses unique evolutionary adaptations for cohabitation with other RiPPs, such as lasso peptides.
  • Specific molecular interactions and discrimination mechanisms prevent cross-reactivity between related biosynthetic pathways.
  • This study enhances our understanding of RiPP evolution and the diversification of natural product biosynthesis.