期刊
MOLECULAR BIOLOGY
卷 54, 期 5, 页码 769-776出版社
PLEIADES PUBLISHING INC
DOI: 10.1134/S0026893320050064
关键词
ribonuclease; binase; pre-steady-state kinetics; fluorescence
资金
- Russian Science Foundation (design and synthesis of RNA substrates, analysis of the enzymatic process by gel electrophoresis and stop flow method) [19-74-10034]
- Russian Foundation for Basic Research [17-0000060]
- Russian State [AAAA-A17-117020210022-4]
- program for improving competitiveness of Kazan (Volga Region) Federal University
- Russian Science Foundation [19-74-10034] Funding Source: Russian Science Foundation
Binase is an extracellular guanyl-preferring ribonuclease fromBacillus 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.
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