Kuznetsova A A, Akhmetgalieva A A, Ulyanova V V, Ilinskaya O N, Fedorova O S, Kuznetsov N A
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences, Novosibirsk, 630090 Russia.
Institute of Fundamental Medicine and Biology, Kazan (Volga Region) Federal University, Kazan, 420008 Russia.
Mol Biol (Mosk). 2020 Sep-Oct;54(5):872-880. doi: 10.31857/S0026898420050067.
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.
Binase是一种来自短小芽孢杆菌的细胞外鸟嘌呤偏好性核糖核酸酶。Binase的主要生物学功能是RNA降解，形成鸟苷-2',3'-环磷酸酯，并随后水解为3'-磷酸酯。细胞外核糖核酸酶被认为是影响机体功能活性的关键因子，因为它们直接与上皮细胞和免疫细胞相互作用。该酶的生物学效应可能既包括直接的RNA降解，也包括人体内2',3'-环鸟苷酸的积累。在这项工作中，我们对模型RNA底物（即含有位于不同位置的鸟苷的短发夹结构）的切割效率进行了比较分析。结果表明，模型RNA底物的水解效率取决于鸟苷的位置。我们还证明了各种二价金属离子和低分子量核苷酸化合物对Binase催化的核糖核酸内切反应的影响。
