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Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis
Fredarla S Miller1, Kathryn K Crone1, Matthew R Jensen2,3
1Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota-Twin Cities, St. Paul, MN, USA.
Nature Communications
|September 10, 2021
Summary
Scientists discovered new
Area of Science:
- Biochemistry and Molecular Biology
- Natural Product Chemistry
Background:
- Peptide backbone α-N-methylations enhance peptide properties like membrane permeability.
- Borosin pathways are the only known ribosomally encoded and post-translationally modified peptides (RiPPs) with backbone α-N-methylations.
Purpose of the Study:
- To discover and characterize novel RiPP pathways with backbone α-N-methylations.
- To investigate the mechanism of iterative maturation in these pathways.
Main Methods:
- Bioinformatic identification of novel RiPP pathways.
- Biochemical characterization of enzyme-substrate interactions.
- Structural analysis using enzyme-precursor complexes.
- Mutational and kinetic analyses.
Main Results:
- Discovery of type IV borosin pathways ('split borosins') in Shewanella oneidensis.
- Identification of an iteratively acting α-N-methyltransferase and a separate precursor peptide.
- Structural insights into enzyme-substrate complex dynamics.
- Functional characterization through mutation and kinetic studies.
Conclusions:
- This study reveals a novel class of RiPP pathways with iterative backbone α-methylation.
- The findings provide insights into the mechanisms of iterative RiPP maturation.
- This work expands the known diversity of RiPP biosynthesis.
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