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Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

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Published on: December 20, 2017

TMcin RiPP biosynthesis in the cellular membrane.

Fauzia H Nur^1,2, Ama N Antwi^1,2, Seth W Dickey^1,2

¹Department of Veterinary Medicine, University of Maryland, College Park, MD, United States of America.

Biorxiv : the Preprint Server for Biology

|June 12, 2026

Summary

This summary is machine-generated.

The cell membrane is the central site for TMcin biosynthesis, a novel class of antimicrobial peptides. This study reveals membrane-localized modifications and provides a model for peptide natural product biosynthesis in a lipid environment.

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Area of Science:

Natural Product Biosynthesis
Molecular Biology
Biotechnology

Background:

Ribosomally synthesized and post-translationally modified peptides (RiPPs) are diverse natural products with therapeutic potential.
Conventional RiPP biosynthesis occurs in aqueous environments, with membrane interaction mainly for secretion.
The TMcin class of RiPPs, featuring a transmembrane helix, represents a newly discovered group with antimicrobial activity.

Purpose of the Study:

To investigate the TMcin class of RiPPs and elucidate their biosynthetic pathway.
To determine the cellular location of TMcin biosynthesis and post-translational modifications.
To establish a model for membrane-localized peptide natural product biosynthesis.

Main Methods:

Utilized an inducible TMcin biosynthesis platform in *Staphylococcus aureus*.
Integrated structure-prediction tools with experimental data.
Characterized gene products from the TMcin biosynthetic gene cluster.

Main Results:

The ribosomally synthesized precursor TmcA is integrated into the producing cell membrane.
All TMcin post-translational modifications occur within the membrane, with three of four mediated by intramembranous proteins.
An uncharacterized membrane protein was assigned an escort function in TMcin biosynthesis.

Conclusions:

The cell membrane serves as the central setting for TMcin biosynthesis, expanding the known scope of RiPP production.
This study provides a novel model for the biosynthesis of membrane-localized peptide natural products.
Findings enable new discoveries and rational engineering of RiPPs, particularly TMcins.