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Vol 54(2020) N 5 p. 769-776; DOI 10.1134/S0026893320050064 Full Text

A.A. Kuznetsova1, A.A. Akhmetgalieva2, V.V. Ulyanova2, O.N. Ilinskaya2, O.S. Fedorova1*, N.A. Kuznetsov1**

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

1Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences, Novosibirsk, 630090 Russia
2Institute of Fundamental Medicine and Biology, Kazan (Volga Region) Federal University, Kazan, 420008 Russia

*fedorova@niboch.nsc.ru
**nikita.kuznetsov@niboch.nsc.ru
Received - 2020-04-13; Revised - 2020-04-28; Accepted - 2020-04-28

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.

ribonuclease, binase, pre-steady-state kinetics, fluorescence



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