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Title: Development of a ribonuclease containing a G4-specific binding motif for programmable RNA cleavage
Authors: Phan, Anh Tuân
Dang, Dung Thanh
Keywords: DRNTU::Science::Physics
Catalytic RNA
Protein Design
Issue Date: 2019
Source: Dang, D. T., & Phan, A. T. (2019). Development of a ribonuclease containing a G4-specific binding motif for programmable RNA cleavage. Scientific Reports, 9(1), 7432-. doi:10.1038/s41598-019-42143-8
Series/Report no.: Scientific Reports
Abstract: We developed a ribonuclease for site-specific targeting and cleavage of single-stranded RNA. The engineered RNase protein was constructed by incorporating two independent functional domains, an RNase HI domain that could cleave the RNA strand in a DNA-RNA hybrid, and a domain of the RHAU protein that could selectively recognize a parallel DNA G-quadruplex (G4). The newly designed RNase first recruits a DNA guide oligonucleotide containing both a parallel G4 motif and a template sequence complementary to the target RNA. This RNase:DNA complex targets and efficiently cleaves the single-stranded RNA in a site-specific manner. A major cleavage site occurs at the RNA region that is complementary to the DNA template sequence. The newly designed RNase can serve as a simple tool for RNA manipulation and probing RNA structure.
DOI: 10.1038/s41598-019-42143-8
Rights: © 2019 The Author(s). 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 license, and indicate if changes were made. Te images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SPMS Journal Articles

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