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Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

13.0K

A Topologically Distinct Modified Peptide with Multiple Bicyclic Core Motifs Expands the Diversity of

Heejin Roh1, Yeji Han1, Hyunbin Lee1

  • 1Department of Chemistry, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul, 08826, South Korea.

Chembiochem : a European Journal of Chemical Biology
|December 22, 2018
PubMed

Insights

Researchers discovered a new group of modified peptides, the thuringinins, which expand the diversity of microviridin-like RiPPs. These peptides feature unique bicyclic structures formed by an ATP-grasp enzyme, suggesting a larger family of omega-ester containing peptides (OEPs).

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Natural Products Chemistry

Background:

  • Microviridins are ribosomally synthesized and post-translationally modified peptides (RiPPs) characterized by multiple intramolecular crosslinks.
  • Most known microviridin-like RiPPs exhibit a single consensus sequence and a tricyclic architecture.

Purpose of the Study:

  • To explore the natural diversity of microviridin-like RiPPs.
  • To determine the crosslinking connectivity of a novel RiPP, mTgnA, and its homologs, termed the thuringinin group.

Main Methods:

  • Determination of crosslinking connectivity for mTgnA and its homologous RiPPs.
  • Analysis of the core motifs and resulting structures of the thuringinin group.

Main Results:

  • Identification of the thuringinin group, a new class of microviridin-like RiPPs with a distinct consensus sequence.
  • Characterization of a novel hairpin-like bicyclic structure formed by a cognate ATP-grasp enzyme.
  • Expansion of the known structural diversity within microviridin-like RiPPs.

Conclusions:

  • The thuringinin group represents a significant expansion of microviridin-like RiPP diversity.
  • These findings suggest a broader family of RiPPs, termed omega-ester containing peptides (OEPs), with novel sequences and architectures.
  • The study highlights the potential for discovering new RiPPs and their unique structures in nature.
Keywords:
ATP-graspRiPPsmacrocyclesmicroviridinpeptides

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