A highly active S1-P1 nuclease from the opportunistic pathogen Stenotrophomonas maltophilia cleaves c-di-GMP.
FEBS Lett
; 597(16): 2103-2118, 2023 08.
Article
em En
| MEDLINE
| ID: mdl-37309731
ABSTRACT
A number of multidrug-resistant bacterial pathogens code for S1-P1 nucleases with a poorly understood role. We have characterized a recombinant form of S1-P1 nuclease from Stenotrophomonas maltophilia, an opportunistic pathogen. S. maltophilia nuclease 1 (SmNuc1) acts predominantly as an RNase and is active in a wide range of temperatures and pH. It retains a notable level of activity towards RNA and ssDNA at pH 5 and 9 and about 10% of activity towards RNA at 10 °C. SmNuc1 with very high catalytic rates outperforms S1 nuclease from Aspergillus oryzae and other similar nucleases on all types of substrates. SmNuc1 degrades second messenger c-di-GMP, which has potential implications for its role in the pathogenicity of S. maltophilia.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Stenotrophomonas maltophilia
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2023
Tipo de documento:
Article
País de afiliação:
República Tcheca