ArticleJournal of molecular biology2006
RNA recognition and cleavage by the SARS coronavirus endoribonuclease.
Article in Journal of molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.
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Who cites it
96 citing papers in PubMed, 160 citations in OpenAlex.
- Coronavirus Nsp15 endoribonuclease: linking viral RNA regulation to immune evasion and viral fitness.Journal of virology · 2026Review
- SARS-CoV-2 EndoU-ribonuclease regulates RNA recombination and impacts viral fitness.Nature communications · 2025Article
- Cleavage sequence specificity of Nsp15.RNA biology · 2025Article
- Assay development and screening of inhibitors targeting the SARS-CoV-2 2'-O-methyltransferase NSP16.Pharmaceutical science advances · 2025Article
- Functional implications of hexameric dynamics in SARS-CoV-2 Nsp15.Protein science : a publication of the Protein Society · 2025Article
- Identification, validation, and characterization of approved and investigational drugs interfering with the SARS-CoV-2 endoribonuclease Nsp15.Protein science : a publication of the Protein Society · 2025Article
- Molecular basis for the calcium-dependent activation of the ribonuclease EndoU.Nature communications · 2025Article
- Identification of acrylamide-based covalent inhibitors of SARS-CoV-2 (SCoV-2) Nsp15 using high-throughput screening and machine learning.RSC advances · 2025Article
- Spontaneous base flipping helps drive Nsp15's preferences in double stranded RNA substrates.Nature communications · 2025Article
- Alternative substrate kinetics of SARS-CoV-2 Nsp15 endonuclease reveals a specificity landscape dominated by RNA structure.Nucleic acids research · 2024Article
- SARS-CoV-2 nsp15 preferentially degrades AU-rich dsRNA via its dsRNA nickase activity.Nucleic acids research · 2024Article
- SARS-CoV-2 nsp15 endoribonuclease antagonizes dsRNA-induced antiviral signaling.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A review of SARS-CoV-2 variants and vaccines: Viral properties, mutations, vaccine efficacy, and safety.Infectious medicine · 2023Review
- Structural basis for polyuridine tract recognition by SARS-CoV-2 Nsp15.bioRxiv : the preprint server for biology · 2023Article
- The endoribonuclease Arlr is required to maintain lipid homeostasis by downregulating lipolytic genes during aging.Nature communications · 2023Article
- Allosteric regulation and crystallographic fragment screening of SARS-CoV-2 NSP15 endoribonuclease.Nucleic acids research · 2023Article
- Room-temperature structural studies of SARS-CoV-2 protein NendoU with an X-ray free-electron laser.Structure (London, England : 1993) · 2023Article
- Article
- Comprehensive Subcellular Localization of Swine Acute Diarrhea Syndrome Coronavirus Proteins.Journal of virology · 2022Article
- Two Years into the COVID-19 Pandemic: Lessons Learned.ACS infectious diseases · 2022Review
36 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The emerging disease SARS is caused by a novel coronavirus that encodes several unusual RNA-processing enzymes, including non-structural protein 15 (Nsp15), a hexameric endoribonuclease that preferentially cleaves at uridine residues. How Nsp15 recognizes and cleaves RNA is not well understood and is the subject of this study. Based on the analysis of RNA products separated by denaturing gel electrophoresis, Nsp15 has been reported to cleave both 5' and 3' of the uridine. We used several RNAs, including some with nucleotide analogs, and mass spectrometry to determine that Nsp15 cleaves only 3' of the recognition uridylate, with some cleavage 3' of cytidylate. A highly conserved RNA structure in the 3' non-translated region of the SARS virus was cleaved preferentially at one of the unpaired uridylate bases, demonstrating that both RNA structure and base-pairing can affect cleavage by Nsp15. Several modified RNAs that are not cleaved by Nsp15 can bind Nsp15 as competitive inhibitors. The RNA binding affinity of Nsp15 increased with the content of uridylate in substrate RNA and the co-factor Mn(2+). The hexameric form of Nsp15 was found to bind RNA in solution. A two-dimensional crystal of Nsp15 in complex with RNA showed that at least two RNA molecules could be bound per hexamer. Furthermore, an 8.3 A structure of Nsp15 was developed using cyroelectron microscopy, allowing us to generate a model of the Nsp15-RNA complex.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.