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

Arnison, Paul G.; Bibb, Mervyn J.; Bierbaum, Gabriele; Bowers, A.; Bugni, Tim S.; Bułaj, Grzegorz; Camarero, Julio A.; Campopiano, Dominic J.; Challis, Gregory L.; Clardy, Jon; Cotter, Paul D.; Craik, David J.; Dawson, Michael J.; Dittmann, Elke; Donadio, Stefano; Dorrestein, Pieter C.; Entian, Karl‐Dieter; Fischbach, Michael A.; Garavelli, John S.; Göransson, Ulf; Gruber, Christian W.; Haft, Daniel H.; Hemscheidt, Thomas; Hertweck, Christian; Hill, Colin; Horswill, Alexander R.; Jaspars, Marcel; Kelly, Walton R.; Klinman, Judith P.; Kuipers, Oscar P.; Link, A. James; Liu, Wen; Marahiel, Mohamed A.; Mitchell, Douglas A.; Moll, Gert N.; Moore, Bradley S.; Müller, Rolf; Nair, Satish K.; Nes, Ingolf F.; Norris, Gillian E.; Olivera, Baldomero M.; Onaka, Hiroyasu; Patchett, Mark L.; Piel, Joern; Reaney, Martin J. T.; Rebuffat, Sylvie; Ross, R. Paul; Sahl, Hans‐Georg; Schmidt, Eric W.; Selsted, Michael E.; Severinov, Konstantin; Shen, Ben; Sivonen, Kaarina; Smith, Linda L.; Stein, Torsten; Süssmuth, Roderich D.; Tagg, John; Tang, Gong‐Li; Truman, Andrew W.; Vederas, John C.; Walsh, Christopher T.; Walton, Jonathan D.; Wenzel, Silke C.; Willey, Joanne M.; Donk, Wilfred A. van der

doi:10.1039/c2np20085f

Cited by 1,696 publications

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“…Moreover, the diverse chemical scaffolds of natural products serve as important starting points in the development of new pharmaceuticals [3]. As a result of large genome-sequencing projects in the past decade, ribosomally synthesized and posttranslationally modified peptides (RiPPs) have recently been recognized as a major class of compounds [4,5]. Extensive post-translational modifications enrich the structural diversity and, thereby, chemical stability and bioactivity of such compounds.…”

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Dual substrate‐controlled kinase activity leads to polyphosphorylated lasso peptides

et al. 2016

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Edited by Alfonso ValenciaLasso peptides are characterized by their peculiar lariat knot-like structure. Except for maturation of this fold, post-translational modifications of lasso peptides are rare. However, we recently delineated the biosynthetic pathway of a post-translationally phosphorylated lasso peptide, paeninodin. In this study, further investigation of two kinases revealed their ability to transfer multiple phosphate groups onto precursor peptide substrates, ultimately leading to polyphosphorylated lasso peptides. We found that this polyphosphorylating activity depended on the identity of the phosphate donor and the sequence of the precursor peptide. Our investigations provide new insight into the remarkable strategies for chemical diversification employed by the lasso peptide biosynthetic machinery.

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confidence: 99%

Dual substrate‐controlled kinase activity leads to polyphosphorylated lasso peptides

et al. 2016

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“…We searched for protein sequences with Cys, Thr, and Ser overrepresented at the C-terminal end and incorporating additional amino acids predicted from our structural analysis, producing a single hit with a short coding sequence ( divA ) for a precursor peptide from a RiPP biosynthetic pathway (Supplementary Table 1). 10 The 20 C-terminal residues of DivA (ARD09202) encompassed the amino acids of 1 predicted by NMR as well as the sequence “GTTK”, suggesting the presence of lysine instead of the predicted arginine. The divA cluster was clearly related to that for the known compound, cinnamycin ( 4 ), a lanthipeptide produced by the soil-actinobacterium Streptomyces cinnamoneous .…”

Section: Resultsmentioning

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“…Lanthionine-containing peptides generally belong to a broad family of ribosomally and posttranslationally modified peptides (RiPPs), 10,11 for which the precursor to the final natural product is genetically encoded. Enzymes act on this ribosomally produced precursor peptide, leading to maturation of a bioactive natural product.…”

Section: Resultsmentioning

confidence: 99%

Accessing chemical diversity from the uncultivated symbionts of small marine animals

et al. 2018

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Chemistry drives many biological interactions between the microbiota and host animals, yet it is often challenging to identify the chemicals involved. This poses a problem, as such small molecules are excellent sources of potential pharmaceuticals, pretested by nature for animal compatibility. We discovered anti-HIV compounds from small, marine tunicates from the Eastern Fields of Papua New Guinea. Tunicates are a reservoir for novel bioactive chemicals, yet their small size often impedes identification or even detection of the chemicals within. We solved this problem by combining chemistry, metagenomics, and synthetic biology to directly identify and synthesize the natural products. We show that these anti-HIV compounds, the divamides, are a novel family of lanthipeptides produced by symbiotic bacteria living in the tunicate. Neighboring animal colonies contain structurally related divamides that differ starkly in their biological properties, suggesting a role for biosynthetic plasticity in a native context where biological interactions take place.

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“…Lasso peptides (LPs) are a rare class of ribosomally synthesized and post-translationally modified peptides (RiPPs) that feature a unique "lariat knot" structural motif (Zimmermann et al 2014;Arnison et al 2013). The post-translational modification includes an isopeptide bond forming a 7-9 amino acid N-terminal macrolactam ring through which the remaining Cterminal chain is threaded (Zimmermann et al 2014).…”

Section: Peptidesmentioning

confidence: 99%

Natural product diversity of actinobacteria in the Atacama Desert

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Jaspars

2018

Antonie van Leeuwenhoek

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The Atacama Desert of northern Chile is considered one of the most arid and extreme environment on Earth. Its core region was described as featuring "Mars-like" soils that were at one point deemed too extreme for life to exist. However, recent investigations confirmed the presence of diverse culturable actinobacteria. In the current review, we discuss a total of 46 natural products isolated to date representing diverse chemical classes characterized from different actinobacteria isolated from various locations in the Atacama Desert. Their reported biological activities are also discussed.

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

Cited by 1,696 publications

References 485 publications

Dual substrate‐controlled kinase activity leads to polyphosphorylated lasso peptides

Dual substrate‐controlled kinase activity leads to polyphosphorylated lasso peptides

Accessing chemical diversity from the uncultivated symbionts of small marine animals

Natural product diversity of actinobacteria in the Atacama Desert

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