Abstract

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.

中文翻译：

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短小芽孢杆菌的联糖酶水解RNA的效率：底物结构，金属离子和低分子量核苷酸化合物的影响

摘要

Binase是来自短小芽孢杆菌的一种细胞外鸟嘌呤核糖核酸酶。Binase的主要生物学功能是RNA降解，形成鸟苷2'，3'-环状磷酸酯并随后水解为3'-磷酸酯。由于细胞外RNase直接与上皮细胞和免疫细胞相互作用，因此被认为是影响人体功能活动的关键物质。该酶的生物学作用可能包括直接的RNA降解和2'，3'-cGMP在人体中的积累。在这项工作中，我们对模型RNA底物的裂解效率进行了比较分析，即在各个位置含有鸟苷的短发夹结构。已经显示出模型RNA底物的水解效率取决于鸟苷的位置。