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Dual RNase and β-lactamase Activity of a Single Enzyme Encoded in Archaea
β-lactam antibiotics have a well-known activity which disturbs the bacterial cell wall biosynthesis and may be cleaved by β-lactamases. However, these drugs are not active on archaea microorganisms, which are naturally resistant because of the lack of β-lactam target in their cell wall. Here, we des...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7697635/ https://www.ncbi.nlm.nih.gov/pubmed/33202677 http://dx.doi.org/10.3390/life10110280 |
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author | Diene, Seydina M. Pinault, Lucile Armstrong, Nicholas Azza, Said Keshri, Vivek Khelaifia, Saber Chabrière, Eric Caetano-Anolles, Gustavo Rolain, Jean-Marc Pontarotti, Pierre Raoult, Didier |
author_facet | Diene, Seydina M. Pinault, Lucile Armstrong, Nicholas Azza, Said Keshri, Vivek Khelaifia, Saber Chabrière, Eric Caetano-Anolles, Gustavo Rolain, Jean-Marc Pontarotti, Pierre Raoult, Didier |
author_sort | Diene, Seydina M. |
collection | PubMed |
description | β-lactam antibiotics have a well-known activity which disturbs the bacterial cell wall biosynthesis and may be cleaved by β-lactamases. However, these drugs are not active on archaea microorganisms, which are naturally resistant because of the lack of β-lactam target in their cell wall. Here, we describe that annotation of genes as β-lactamases in Archaea on the basis of homologous genes is a remnant of identification of the original activities of this group of enzymes, which in fact have multiple functions, including nuclease, ribonuclease, β-lactamase, or glyoxalase, which may specialized over time. We expressed class B β-lactamase enzyme from Methanosarcina barkeri that digest penicillin G. Moreover, while weak glyoxalase activity was detected, a significant ribonuclease activity on bacterial and synthetic RNAs was demonstrated. The β-lactamase activity was inhibited by β-lactamase inhibitor (sulbactam), but its RNAse activity was not. This gene appears to have been transferred to the Flavobacteriaceae group especially the Elizabethkingia genus, in which the expressed gene shows a more specialized activity on thienamycin, but no glyoxalase activity. The expressed class C-like β-lactamase gene, from Methanosarcina sp., also shows hydrolysis activity on nitrocefin and is more closely related to DD-peptidase enzymes. Our findings highlight the need to redefine the nomenclature of β-lactamase enzymes and the specification of multipotent enzymes in different ways in Archaea and bacteria over time. |
format | Online Article Text |
id | pubmed-7697635 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-76976352020-11-29 Dual RNase and β-lactamase Activity of a Single Enzyme Encoded in Archaea Diene, Seydina M. Pinault, Lucile Armstrong, Nicholas Azza, Said Keshri, Vivek Khelaifia, Saber Chabrière, Eric Caetano-Anolles, Gustavo Rolain, Jean-Marc Pontarotti, Pierre Raoult, Didier Life (Basel) Article β-lactam antibiotics have a well-known activity which disturbs the bacterial cell wall biosynthesis and may be cleaved by β-lactamases. However, these drugs are not active on archaea microorganisms, which are naturally resistant because of the lack of β-lactam target in their cell wall. Here, we describe that annotation of genes as β-lactamases in Archaea on the basis of homologous genes is a remnant of identification of the original activities of this group of enzymes, which in fact have multiple functions, including nuclease, ribonuclease, β-lactamase, or glyoxalase, which may specialized over time. We expressed class B β-lactamase enzyme from Methanosarcina barkeri that digest penicillin G. Moreover, while weak glyoxalase activity was detected, a significant ribonuclease activity on bacterial and synthetic RNAs was demonstrated. The β-lactamase activity was inhibited by β-lactamase inhibitor (sulbactam), but its RNAse activity was not. This gene appears to have been transferred to the Flavobacteriaceae group especially the Elizabethkingia genus, in which the expressed gene shows a more specialized activity on thienamycin, but no glyoxalase activity. The expressed class C-like β-lactamase gene, from Methanosarcina sp., also shows hydrolysis activity on nitrocefin and is more closely related to DD-peptidase enzymes. Our findings highlight the need to redefine the nomenclature of β-lactamase enzymes and the specification of multipotent enzymes in different ways in Archaea and bacteria over time. MDPI 2020-11-14 /pmc/articles/PMC7697635/ /pubmed/33202677 http://dx.doi.org/10.3390/life10110280 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Diene, Seydina M. Pinault, Lucile Armstrong, Nicholas Azza, Said Keshri, Vivek Khelaifia, Saber Chabrière, Eric Caetano-Anolles, Gustavo Rolain, Jean-Marc Pontarotti, Pierre Raoult, Didier Dual RNase and β-lactamase Activity of a Single Enzyme Encoded in Archaea |
title | Dual RNase and β-lactamase Activity of a Single Enzyme Encoded in Archaea |
title_full | Dual RNase and β-lactamase Activity of a Single Enzyme Encoded in Archaea |
title_fullStr | Dual RNase and β-lactamase Activity of a Single Enzyme Encoded in Archaea |
title_full_unstemmed | Dual RNase and β-lactamase Activity of a Single Enzyme Encoded in Archaea |
title_short | Dual RNase and β-lactamase Activity of a Single Enzyme Encoded in Archaea |
title_sort | dual rnase and β-lactamase activity of a single enzyme encoded in archaea |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7697635/ https://www.ncbi.nlm.nih.gov/pubmed/33202677 http://dx.doi.org/10.3390/life10110280 |
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