Affiliation:
1. Laboratory of Structure and Function of Biomolecules, Institute of Biotechnology of the Czech Academy of Sciences Biocev Vestec Czech Republic
2. Department of Biochemistry and Microbiology University of Chemistry and Technology Prague Czech Republic
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.
Funder
Akademie Věd České Republiky
European Regional Development Fund
Grantová Agentura České Republiky
Ministerstvo Školství, Mládeže a Tělovýchovy
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics