A highly active S1-P1 nuclease from the opportunistic pathogen iStenotrophomonas maltophilia/i cleaves c-di-GMP

0583248 - BTÚ 2024 RIV US eng J - Journal Article
Husťáková, Blanka - Trundová, Mária - Adámková, Kristýna - Koval, Tomáš - Dušková, Jarmila - Dohnálek, Jan
A highly active S1-P1 nuclease from the opportunistic pathogen iStenotrophomonas maltophilia/i cleaves c-di-GMP.
FEBS Letters. Roč. 597, č. 16 (2023), s. 2103-2118. ISSN 0014-5793. E-ISSN 1873-3468
R&D Projects: GA ČR(CZ) GA20-12109S; GA MŠMT EF15_003/0000447
Research Infrastructure: CIISB III - 90242
Institutional support: RVO:86652036
Keywords : n-glycosylation * phosphodiesterase * mechanism * enzyme * S1-P1 nuclease
OECD category: Biophysics
Impact factor: 3.5, year: 2022
Method of publishing: Open access
https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.14683

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 degrees C. SmNuc1 with very high catalytic rates out-performs 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.
Permanent Link: https://hdl.handle.net/11104/0351252