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

Sikandar, A. and Koehnke, J. (2019) The role of protein–protein interactions in the biosynthesis of ribosomally synthesized and post-translationally modified peptides. Natural Product Reports, 36, pp. 1576-1588. (doi: 10.1039/C8NP00064F) (PMID:30920567)

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Abstract

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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Koehnke, Professor Jesko
Authors: Sikandar, A., and Koehnke, J.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Natural Product Reports
Publisher:Royal Society of Chemistry
ISSN:0265-0568
ISSN (Online):1460-4752

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