TY - JOUR
T1 - Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides
AU - Ongpipattanakul, Chayanid
AU - Desormeaux, Emily K.
AU - Dicaprio, Adam
AU - Van Der Donk, Wilfred A.
AU - Mitchell, Douglas A.
AU - Nair, Satish K.
N1 - Funding Information:
We thank the National Institutes of Health (R37 GM058822 to W.A.V, R01 AI144967 to D.A.M and W.A.V, GM131347 and GM079038 to S.K.N., and GM123998 to D.A.M) and the Howard Hughes Medical Institute (W.A.V) for funding our programs on RiPPs.
Publisher Copyright:
© 2022 American Chemical Society. All rights reserved.
PY - 2022/9/28
Y1 - 2022/9/28
N2 - Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a natural product class that has undergone significant expansion due to the rapid growth in genome sequencing data and recognition that they are made by biosynthetic pathways that share many characteristic features. Their mode of actions cover a wide range of biological processes and include binding to membranes, receptors, enzymes, lipids, RNA, and metals as well as use as cofactors and signaling molecules. This review covers the currently known modes of action (MOA) of RiPPs. In turn, the mechanisms by which these molecules interact with their natural targets provide a rich set of molecular paradigms that can be used for the design or evolution of new or improved activities given the relative ease of engineering RiPPs. In this review, coverage is limited to RiPPs originating from bacteria.
AB - Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a natural product class that has undergone significant expansion due to the rapid growth in genome sequencing data and recognition that they are made by biosynthetic pathways that share many characteristic features. Their mode of actions cover a wide range of biological processes and include binding to membranes, receptors, enzymes, lipids, RNA, and metals as well as use as cofactors and signaling molecules. This review covers the currently known modes of action (MOA) of RiPPs. In turn, the mechanisms by which these molecules interact with their natural targets provide a rich set of molecular paradigms that can be used for the design or evolution of new or improved activities given the relative ease of engineering RiPPs. In this review, coverage is limited to RiPPs originating from bacteria.
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U2 - 10.1021/acs.chemrev.2c00210
DO - 10.1021/acs.chemrev.2c00210
M3 - Review article
C2 - 36049139
AN - SCOPUS:85138059541
SN - 0009-2665
VL - 122
SP - 14722
EP - 14814
JO - Chemical Reviews
JF - Chemical Reviews
IS - 18
ER -