Laboratory of Structure and Function of Biomolecules, Institute of Biotechnology of the Czech Academy of Sciences, Biocev, Vestec, Czech Republic.
Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.
FEBS Lett. 2023 Aug;597(16):2103-2118. doi: 10.1002/1873-3468.14683. Epub 2023 Jun 19.
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.
许多多药耐药细菌病原体编码具有未知作用的 S1-P1 核酸酶。我们已经对来自嗜麦芽寡养单胞菌的 S1-P1 核酸酶的重组形式进行了表征，嗜麦芽寡养单胞菌是一种机会性病原体。S. maltophilia nuclease 1 (SmNuc1) 主要作为 RNase 起作用，并在广泛的温度和 pH 值范围内具有活性。它在 pH 值为 5 和 9 时对 RNA 和 ssDNA 保持显著的活性，在 10°C 时对 RNA 的活性约为 10%。SmNuc1 的催化速率非常高，在所有类型的底物上的表现均优于来自米曲霉和其他类似核酸酶的 S1 核酸酶。SmNuc1 降解第二信使 c-di-GMP，这可能与其在嗜麦芽寡养单胞菌致病性中的作用有关。
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