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Identification of a solo acylhomoserine lactone synthase from the myxobacterium Archangium gephyra
Considered a key taxon in soil and marine microbial communities, myxobacteria exist as coordinated swarms that utilize a combination of lytic enzymes and specialized metabolites to facilitate predation of microbes. This capacity to produce specialized metabolites and the associated abundance of bios...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7862692/ https://www.ncbi.nlm.nih.gov/pubmed/33542315 http://dx.doi.org/10.1038/s41598-021-82480-1 |
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author | Albataineh, Hanan Duke, Maya Misra, Sandeep K. Sharp, Joshua S. Stevens, D. Cole |
author_facet | Albataineh, Hanan Duke, Maya Misra, Sandeep K. Sharp, Joshua S. Stevens, D. Cole |
author_sort | Albataineh, Hanan |
collection | PubMed |
description | Considered a key taxon in soil and marine microbial communities, myxobacteria exist as coordinated swarms that utilize a combination of lytic enzymes and specialized metabolites to facilitate predation of microbes. This capacity to produce specialized metabolites and the associated abundance of biosynthetic pathways contained within their genomes have motivated continued drug discovery efforts from myxobacteria. Of all myxobacterial biosynthetic gene clusters deposited in the antiSMASH database, only one putative acylhomoserine lactone (AHL) synthase, agpI, was observed, in genome data from Archangium gephyra. Without an AHL receptor also apparent in the genome of A. gephyra, we sought to determine if AgpI was an uncommon example of an orphaned AHL synthase. Herein we report the bioinformatic assessment of AgpI and discovery of a second AHL synthase from Vitiosangium sp. During axenic cultivation conditions, no detectible AHL metabolites were observed in A. gephyra extracts. However, heterologous expression of each synthase in Escherichia coli provided detectible quantities of 3 AHL signals including 2 known AHLs, C8-AHL and C9-AHL. These results suggest that A. gephyra AHL production is dormant during axenic cultivation. The functional, orphaned AHL synthase, AgpI, is unique to A. gephyra, and its utility to the predatory myxobacterium remains unknown. |
format | Online Article Text |
id | pubmed-7862692 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-78626922021-02-08 Identification of a solo acylhomoserine lactone synthase from the myxobacterium Archangium gephyra Albataineh, Hanan Duke, Maya Misra, Sandeep K. Sharp, Joshua S. Stevens, D. Cole Sci Rep Article Considered a key taxon in soil and marine microbial communities, myxobacteria exist as coordinated swarms that utilize a combination of lytic enzymes and specialized metabolites to facilitate predation of microbes. This capacity to produce specialized metabolites and the associated abundance of biosynthetic pathways contained within their genomes have motivated continued drug discovery efforts from myxobacteria. Of all myxobacterial biosynthetic gene clusters deposited in the antiSMASH database, only one putative acylhomoserine lactone (AHL) synthase, agpI, was observed, in genome data from Archangium gephyra. Without an AHL receptor also apparent in the genome of A. gephyra, we sought to determine if AgpI was an uncommon example of an orphaned AHL synthase. Herein we report the bioinformatic assessment of AgpI and discovery of a second AHL synthase from Vitiosangium sp. During axenic cultivation conditions, no detectible AHL metabolites were observed in A. gephyra extracts. However, heterologous expression of each synthase in Escherichia coli provided detectible quantities of 3 AHL signals including 2 known AHLs, C8-AHL and C9-AHL. These results suggest that A. gephyra AHL production is dormant during axenic cultivation. The functional, orphaned AHL synthase, AgpI, is unique to A. gephyra, and its utility to the predatory myxobacterium remains unknown. Nature Publishing Group UK 2021-02-04 /pmc/articles/PMC7862692/ /pubmed/33542315 http://dx.doi.org/10.1038/s41598-021-82480-1 Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Albataineh, Hanan Duke, Maya Misra, Sandeep K. Sharp, Joshua S. Stevens, D. Cole Identification of a solo acylhomoserine lactone synthase from the myxobacterium Archangium gephyra |
title | Identification of a solo acylhomoserine lactone synthase from the myxobacterium Archangium gephyra |
title_full | Identification of a solo acylhomoserine lactone synthase from the myxobacterium Archangium gephyra |
title_fullStr | Identification of a solo acylhomoserine lactone synthase from the myxobacterium Archangium gephyra |
title_full_unstemmed | Identification of a solo acylhomoserine lactone synthase from the myxobacterium Archangium gephyra |
title_short | Identification of a solo acylhomoserine lactone synthase from the myxobacterium Archangium gephyra |
title_sort | identification of a solo acylhomoserine lactone synthase from the myxobacterium archangium gephyra |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7862692/ https://www.ncbi.nlm.nih.gov/pubmed/33542315 http://dx.doi.org/10.1038/s41598-021-82480-1 |
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