Dual RNase and β-lactamase Activity of a Single Enzyme Encoded in Archaea

Autor: Seydina M. Diene, Lucile Pinault, Nicholas Armstrong, Said Azza, Vivek Keshri, Saber Khelaifia, Eric Chabrière, Gustavo Caetano-Anolles, Jean-Marc Rolain, Pierre Pontarotti, Didier Raoult
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Zdroj: Life, Vol 10, Iss 11, p 280 (2020)
Druh dokumentu: article
ISSN: 2075-1729
59420480
DOI: 10.3390/life10110280
Popis: 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.
Databáze: Directory of Open Access Journals
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