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The role of protein–protein interactions in the biosynthesis of ribosomally synthesized and post-translationally modified peptides

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Abstract

Covering: up to 02/2019

This review covers the role of protein–protein complexes in the biosynthesis of selected ribosomally synthesized and post-translationally modified peptide (RiPP) classes. The genomic organization of RiPP systems usually allows the expression of each biosynthetic enzyme as an individual unit, which is in stark contrast to the giant assembly lines found in non-ribosomal peptide and polyketide synthesis systems. Evidence is mounting however that the formation of multi-enzyme complexes is critical for efficient RiPPs biosynthesis and that these complexes may be involved in substrate channeling or conformational sampling. In some pathways, polyfunctional enzymes have evolved, which can be viewed as perpetual protein complexes. We summarize what is currently known on enzyme complexes in RiPP systems for lasso peptides, cyanobactins, linear azolic peptides, thiopeptides, and lanthipeptides.

Graphical abstract: The role of protein–protein interactions in the biosynthesis of ribosomally synthesized and post-translationally modified peptides

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Publication details

The article was received on 12 Jul 2018 and first published on 28 Mar 2019


Article type: Review Article
DOI: 10.1039/C8NP00064F
Nat. Prod. Rep., 2019, Advance Article

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    The role of protein–protein interactions in the biosynthesis of ribosomally synthesized and post-translationally modified peptides

    A. Sikandar and J. Koehnke, Nat. Prod. Rep., 2019, Advance Article , DOI: 10.1039/C8NP00064F

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