ArticleScientific reports2019
Development of a ribonuclease containing a G4-specific binding motif for programmable RNA cleavage.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Specific binding of G-quadruplex in SARS-CoV-2 RNA by RHAU peptide.Current research in structural biology · 2024Article
- DNA G-Quadruplex-Binding Protein Developed Using the RGG Domain of Translocated in Liposarcoma/Fused in Sarcoma Inhibits Transcription ofACS omega · 2023Article
- BioCRNpyler: Compiling chemical reaction networks from biomolecular parts in diverse contexts.PLoS computational biology · 2022Article
- Molecular Approaches to Protein Dimerization: Opportunities for Supramolecular Chemistry.Frontiers in chemistry · 2022Review
- Parallel G-quadruplex-mediated protein dimerization and activation.RSC advances · 2020Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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