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. 2024 Jun 28;14:14973. doi: 10.1038/s41598-024-65814-7

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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hEndoV prefers a hydroxy (–OH) modification of adenosine. (A) ³²P-labeled substrates containing deoxyinosine and a series of adenosine modifications are shown. Intact 21-nt; Intact oligonucleotide. Product 12-nt; cleavage products. (B) ³²P-labeled substrate containing deoxyinosine and rAAA (lanes 1–4), rArAA (lanes 5–8) and rArArA (lanes 9–12) were incubated with 5 nM hEndoV at 37 ℃ for 0, 5, 15 and 30 min. (C) The cleavage products were analyzed by denaturing 12.5% urea gel electrophorese. (D) Preference of chemical structure in hEndoV cleavage activity. Abbreviations: hEndoV, human endonuclease V; P, phosphorus; rA, ribo-adenine; dI, deoxyinosine; A, deoxy-adenine Representatives of three independent experiments are shown.