TY - JOUR
T1 - New developments in RiPP discovery, enzymology and engineering
AU - Montalbán-López, Manuel
AU - Scott, Thomas A.
AU - Ramesh, Sangeetha
AU - Rahman, Imran R.
AU - Van Heel, Auke J.
AU - Viel, Jakob H.
AU - Bandarian, Vahe
AU - Dittmann, Elke
AU - Genilloud, Olga
AU - Goto, Yuki
AU - Grande Burgos, María José
AU - Hill, Colin
AU - Kim, Seokhee
AU - Koehnke, Jesko
AU - Latham, John A.
AU - Link, A. James
AU - Martínez, Beatriz
AU - Nair, Satish K.
AU - Nicolet, Yvain
AU - Rebuffat, Sylvie
AU - Sahl, Hans Georg
AU - Sareen, Dipti
AU - Schmidt, Eric W.
AU - Schmitt, Lutz
AU - Severinov, Konstantin
AU - Süssmuth, Roderich D.
AU - Truman, Andrew W.
AU - Wang, Huan
AU - Weng, Jing Ke
AU - Van Wezel, Gilles P.
AU - Zhang, Qi
AU - Zhong, Jin
AU - Piel, Jörn
AU - Mitchell, Douglas A.
AU - Kuipers, Oscar P.
AU - Van Der Donk, Wilfred A.
N1 - Funding Information:
RiPP research in the laboratories of the corresponding authors is supported by grants from the National Institutes of Health (GM123998 to DAM, AI144967 to WAV and DAM, GM058822 to WAV, and 5T32-GM070421 to IRR), the EU FW7 programme SynPeptide (to MML, OPK and JP), the EU Horizon 2020 programme Ras4Biotech (to AJvH), the Swiss National Science Foundation (407240_1167051 to JP), the Dutch Research Council (NWO-ALWOP-214 to JV), a European Molecular Biology Organization Long-Term Fellowship (ALTF 344-2018 to TAS), and the Howard Hughes Medical Institute (to WAV).
Publisher Copyright:
© The Royal Society of Chemistry.
PY - 2021
Y1 - 2021
N2 - Covering: up to June 2020 Ribosomally-synthesized and post-translationally modified peptides (RiPPs) are a large group of natural products. A community-driven review in 2013 described the emerging commonalities in the biosynthesis of RiPPs and the opportunities they offered for bioengineering and genome mining. Since then, the field has seen tremendous advances in understanding of the mechanisms by which nature assembles these compounds, in engineering their biosynthetic machinery for a wide range of applications, and in the discovery of entirely new RiPP families using bioinformatic tools developed specifically for this compound class. The First International Conference on RiPPs was held in 2019, and the meeting participants assembled the current review describing new developments since 2013. The review discusses the new classes of RiPPs that have been discovered, the advances in our understanding of the installation of both primary and secondary post-translational modifications, and the mechanisms by which the enzymes recognize the leader peptides in their substrates. In addition, genome mining tools used for RiPP discovery are discussed as well as various strategies for RiPP engineering. An outlook section presents directions for future research.
AB - Covering: up to June 2020 Ribosomally-synthesized and post-translationally modified peptides (RiPPs) are a large group of natural products. A community-driven review in 2013 described the emerging commonalities in the biosynthesis of RiPPs and the opportunities they offered for bioengineering and genome mining. Since then, the field has seen tremendous advances in understanding of the mechanisms by which nature assembles these compounds, in engineering their biosynthetic machinery for a wide range of applications, and in the discovery of entirely new RiPP families using bioinformatic tools developed specifically for this compound class. The First International Conference on RiPPs was held in 2019, and the meeting participants assembled the current review describing new developments since 2013. The review discusses the new classes of RiPPs that have been discovered, the advances in our understanding of the installation of both primary and secondary post-translational modifications, and the mechanisms by which the enzymes recognize the leader peptides in their substrates. In addition, genome mining tools used for RiPP discovery are discussed as well as various strategies for RiPP engineering. An outlook section presents directions for future research.
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U2 - 10.1039/d0np00027b
DO - 10.1039/d0np00027b
M3 - Review article
C2 - 32935693
AN - SCOPUS:85101053260
SN - 0265-0568
VL - 38
SP - 130
EP - 239
JO - Natural Product Reports
JF - Natural Product Reports
IS - 1
ER -