Efficiency of RNA Hydrolysis by Binase from Bacillus pumilus: The Impact of Substrate Structure, Metal Ions, and Low Molecular Weight Nucleotide Compounds

• Published in: Molecular biology (New York) Vol. 54; no. 5; pp. 769 - 776
• Main Authors: Kuznetsova, A. A., Akhmetgalieva, A. A., Ulyanova, V. V., Ilinskaya, O. N., Fedorova, O. S., Kuznetsov, N. A.
• Format: Journal Article
• Language: English
• Published: Moscow Pleiades Publishing 01.09.2020; Springer Nature B.V
• Subjects: Bacillus pumilus; Biochemistry; Biomedical and Life Sciences; Comparative analysis; Cyclic GMP; Efficiency; Guanosine; Human Genetics; Hydrolysis; Life Sciences; Metal ions; Molecular weight; Ribonuclease; Ribonucleic acid; RNA; Structural-Functional Analysis of Biopolymers and Their Complexes; binase; pre-steady-state kinetics; fluorescence; ribonuclease
• ISSN: 0026-8933; 1608-3245
• DOI: 10.1134/S0026893320050064

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.