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How a Subfamily of Radical S-Adenosylmethionine Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally Modified Peptide Discovery
[Image: see text] Radical S-adenosylmethionine (rSAM) enzymes are a large and diverse superfamily of enzymes, some of which are known to participate in the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs). Specifically, a subfamily of rSAM proteins with an e...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10114670/ https://www.ncbi.nlm.nih.gov/pubmed/37102180 http://dx.doi.org/10.1021/acsbiomedchemau.1c00045 |
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author | Mendauletova, Aigera Kostenko, Anastasiia Lien, Yi Latham, John |
author_facet | Mendauletova, Aigera Kostenko, Anastasiia Lien, Yi Latham, John |
author_sort | Mendauletova, Aigera |
collection | PubMed |
description | [Image: see text] Radical S-adenosylmethionine (rSAM) enzymes are a large and diverse superfamily of enzymes, some of which are known to participate in the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs). Specifically, a subfamily of rSAM proteins with an elongated C-terminus known as a SPASM domain have become a fixation in the discovery of new RiPP natural products. Arguably, a structural study, a bioinformatic study, and a functional study built the foundation of the research for rSAM-SPASM-protein-modified RiPPs. In this Review, we focus on these three studies and how they initiated what has become an increasingly productive field. In addition, we discuss the current state of RiPPs that depends on rSAM-SPASM proteins and provide guidelines to consider in future research. Lastly, we discuss how genome mining tools have become a powerful means to identify and predict new RiPP natural products. Despite the state of our current knowledge, we do not completely understand the relationship of rSAM-SPASM chemistry, substrate recognition, and the structure–function relationship as it pertains to RiPP biosynthesis, and as such, there remain many interesting findings waiting to be discovered in the future. |
format | Online Article Text |
id | pubmed-10114670 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-101146702023-04-25 How a Subfamily of Radical S-Adenosylmethionine Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally Modified Peptide Discovery Mendauletova, Aigera Kostenko, Anastasiia Lien, Yi Latham, John ACS Bio Med Chem Au [Image: see text] Radical S-adenosylmethionine (rSAM) enzymes are a large and diverse superfamily of enzymes, some of which are known to participate in the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs). Specifically, a subfamily of rSAM proteins with an elongated C-terminus known as a SPASM domain have become a fixation in the discovery of new RiPP natural products. Arguably, a structural study, a bioinformatic study, and a functional study built the foundation of the research for rSAM-SPASM-protein-modified RiPPs. In this Review, we focus on these three studies and how they initiated what has become an increasingly productive field. In addition, we discuss the current state of RiPPs that depends on rSAM-SPASM proteins and provide guidelines to consider in future research. Lastly, we discuss how genome mining tools have become a powerful means to identify and predict new RiPP natural products. Despite the state of our current knowledge, we do not completely understand the relationship of rSAM-SPASM chemistry, substrate recognition, and the structure–function relationship as it pertains to RiPP biosynthesis, and as such, there remain many interesting findings waiting to be discovered in the future. American Chemical Society 2021-12-02 /pmc/articles/PMC10114670/ /pubmed/37102180 http://dx.doi.org/10.1021/acsbiomedchemau.1c00045 Text en © 2021 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Mendauletova, Aigera Kostenko, Anastasiia Lien, Yi Latham, John How a Subfamily of Radical S-Adenosylmethionine Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally Modified Peptide Discovery |
title | How a Subfamily of Radical S-Adenosylmethionine
Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally
Modified Peptide Discovery |
title_full | How a Subfamily of Radical S-Adenosylmethionine
Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally
Modified Peptide Discovery |
title_fullStr | How a Subfamily of Radical S-Adenosylmethionine
Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally
Modified Peptide Discovery |
title_full_unstemmed | How a Subfamily of Radical S-Adenosylmethionine
Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally
Modified Peptide Discovery |
title_short | How a Subfamily of Radical S-Adenosylmethionine
Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally
Modified Peptide Discovery |
title_sort | how a subfamily of radical s-adenosylmethionine
enzymes became a mainstay of ribosomally synthesized and post-translationally
modified peptide discovery |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10114670/ https://www.ncbi.nlm.nih.gov/pubmed/37102180 http://dx.doi.org/10.1021/acsbiomedchemau.1c00045 |
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