Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.

@article{Arnison2013RibosomallySA,
  title={Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.},
  author={Paul G. Arnison and Mervyn J. Bibb and Gabriele Bierbaum and Albert A Bowers and Tim S. Bugni and Grzegorz Bulaj and Julio A. Camarero and Dominic J. Campopiano and Gregory L. Challis and Jon Clardy and Paul D. Cotter and David J. Craik and Michael Dawson and Elke Dittmann and Stefano Donadio and Pieter C. Dorrestein and Karl-D. Entian and Michael A. Fischbach and John S. Garavelli and Ulf G{\"o}ransson and Christian W. Gruber and Daniel H. Haft and Thomas K. Hemscheidt and C. Hertweck and Colin Hill and Alexander R. Horswill and Marcel Jaspars and Wendy L Kelly and Judith P Klinman and Oscar P. Kuipers and A. James Link and Wen Liu and Mohamed A. Marahiel and Douglas A. Mitchell and Gert N Moll and Bradley S. Moore and Rolf M{\"u}ller and Satish K. Nair and Ingolf F. Nes and Gillian E Norris and Baldomero M. Olivera and Hiroyasu Onaka and Mark L. Patchett and Joern Piel and Martin J. T. Reaney and Sylvie Rebuffat and Reynolds Paul Ross and H. -G. Sahl and Eric W. Schmidt and Michael E. Selsted and Konstantin V. Severinov and Ben Shen and Kaarina Sivonen and Leif Smith and Torsten Stein and Roderich D. S{\"u}ssmuth and John R. Tagg and Gong-Li Tang and Andrew W. Truman and John C. Vederas and Christopher T Walsh and Jonathan D. Walton and Silke C Wenzel and Joanne M. Willey and Wilfred A. van der Donk},
  journal={Natural product reports},
  year={2013},
  volume={30 1},
  pages={
          108-60
        }
}
This review presents recommended nomenclature for the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs), a rapidly growing class of natural products. The current knowledge regarding the biosynthesis of the >20 distinct compound classes is also reviewed, and commonalities are discussed. 
New Insights into the Biosynthetic Logic of Ribosomally Synthesized and Post-translationally Modified Peptide Natural Products.
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This Review highlights recent developments in the understanding of the biosynthesis of several bacterial RiPP family members, the use of the RiPP biosynthetic machinery for generating novel macrocyclic peptides, and the implementation of tools designed to guide the discovery and characterization of novel RiPPs. Expand
Expanding the Structural Space of Ribosomal Peptides: Autocatalytic N-Methylation in Omphalotin Biosynthesis.
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Tail-Me: The N-methylation of backbone amide bonds in peptide natural products was thought to be exclusive to non-ribosomal peptides, but a newly discovered methylation mechanism now brings this structural feature into the world of ribosomally synthesized and post-translationally modified peptides (RiPPs). Expand
Ribosomally synthesized and post-translationally modified peptide natural products: new insights into the role of leader and core peptides during biosynthesis.
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It is proposed that the leader peptides function as allosteric regulators that bind the active form of the biosynthetic enzymes in a conformational selection process, and how enzymes that generate polycyclic products of defined topologies may have been selected for during evolution. Expand
Decoding and recoding the ribosomal peptide universe.
  • E. Schmidt
  • Medicine, Biology
  • Chemistry & biology
  • 2012
TLDR
In this issue of Chemistry & Biology, Young and colleagues overcome hurdles that have slowed the development of RiPPs, leading to in vivo synthesis of new thiopeptide antibiotics. Expand
Unveiling the Biosynthetic Pathway of the Ribosomally Synthesized and Post-translationally Modified Peptide Ustiloxin B in Filamentous Fungi.
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The biosynthetic machinery of the first fungal ribosomally synthesized and post-translationally modified peptide (RiPP) ustiloxin B was elucidated through a series of gene inactivation and heterologous expression studies, providing new insight into the expression of the RiPP gene clusters found in various fungi. Expand
Mechanisms of action of ribosomally synthesized and posttranslationally modified peptides (RiPPs)
TLDR
This review highlights examples of the molecular mechanisms of action of RiPPs: ribosomally synthesized and posttranslationally modified peptides that underly those bioactivities. Expand
Enzymatic macrocyclization of ribosomally synthesized and posttranslational modified peptides via C-S and C-C bond formation.
TLDR
Recent progress in the macrocyclization of RiPPs by C-S and C-C bond formation is summarized with a focus on the current understanding of the enzymatic mechanisms. Expand
Structure and mechanism of lanthipeptide biosynthetic enzymes.
TLDR
Structural studies have started to provide insights into recognition of the peptide substrates by the modification enzymes, and unexpected mechanisms of the post-translational modifications are revealed. Expand
Ribosomally synthesized and post-translationally modified peptide natural product discovery in the genomic era.
TLDR
This review highlights applications of genome mining software to compare and organize large-scale data sets and methods for identifying unique biosynthetic pathways amongst the thousands of ribosomally synthesized and post-translationally modified peptide (RiPP) gene clusters. Expand
Structural Biology of RiPP Natural Products Biosynthesis
Abstract Over the past two decades, there have been significant advances in the understanding of enzymes that carry out the biosynthesis of ribosomally synthesized and posttranslationally modifiedExpand
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