Efficiency of RNA Hydrolysis by Binase from Bacillus pumilus: The Impact of Substrate Structure, Metal Ions, and Low Molecular Weight Nucleotide Compounds
| Autor: | Alexandra A. Kuznetsova, Olga S. Fedorova, Nikita A. Kuznetsov, A A Akhmetgalieva, Olga N. Ilinskaya, Vera Ulyanova |
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| Rok vydání: | 2020 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences biology Bacillus pumilus 030302 biochemistry & molecular biology Biophysics RNA Guanosine biology.organism_classification RNA hydrolysis 03 medical and health sciences Hydrolysis chemistry.chemical_compound Enzyme chemistry Biochemistry Structural Biology biology.protein Nucleotide Ribonuclease |
| Zdroj: | Molecular Biology. 54:769-776 |
| ISSN: | 1608-3245 0026-8933 |
| DOI: | 10.1134/s0026893320050064 |
| Popis: | Binase is an extracellular guanyl-preferring ribonuclease from Bacillus pumilus. The main biological function of binase is RNA degradation with the formation of guanosine-2',3'-cyclic phosphate and its subsequent hydrolysis to 3'-phosphate. Extracellular RNases are believed to be key agents that affect the functional activity of the body, as they directly interact with epithelial and immune cells. The biological effects of the enzyme may consist of both direct RNA degradation, and the accumulation of 2',3'-cGMP in the human body. In this work, we have performed a comparative analysis of the cleavage efficiency of model RNA substrates, i.e., short hairpin structures that contain guanosine at various positions. It has been shown that the hydrolysis efficiency of the model RNA substrates depends on the position of guanosine. We have also demonstrated the influence of various divalent metal ions and low molecular weight nucleotide compounds on the binase-catalyzed endoribonucleolytic reaction. |
| Databáze: | OpenAIRE |
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