ArticleJournal of molecular biology2006
Histidine triad-like motif of the rotavirus NSP2 octamer mediates both RTPase and NTPase activities.
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 24 papers.
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Who cites it
24 citing papers in PubMed, 51 citations in OpenAlex.
- K294E change in the rotavirus factory forming protein NSP2 stabilizes a rare C-terminal conformation.Journal of biomolecular structure & dynamics · 2026Article
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- Cryo-EM structure of rotavirus B NSP2 reveals its unique tertiary architecture.Journal of virology · 2024Article
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- Structural basis of rotavirus RNA chaperone displacement and RNA annealing.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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- 2.7 Å cryo-EM structure of rotavirus core protein VP3, a unique capping machine with a helicase activity.Science advances · 2020Article
- Phosphorylation cascade regulates the formation and maturation of rotaviral replication factories.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Probing the sites of interactions of rotaviral proteins involved in replication.Journal of virology · 2014Article
- The viral RNA capping machinery as a target for antiviral drugs.Antiviral research · 2012Review
- Crystallographic Analysis of Rotavirus NSP2-RNA Complex Reveals Specific Recognition of 5' GG Sequence for RTPase Activity.Journal of virology · 2012Article
- Rotavirus non-structural proteins: structure and function.Current opinion in virology · 2012Review
- Vaccine-derived NSP2 segment in rotaviruses from vaccinated children with gastroenteritis in Nicaragua.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2012Article
- Crystallographic analysis reveals octamerization of viroplasm matrix protein P9-1 of Rice black streaked dwarf virus.Journal of virology · 2012Article
- Conventional and unconventional mechanisms for capping viral mRNA.Nature reviews. Microbiology · 2011Review
- Rice black-streaked dwarf virus P6 self-interacts to form punctate, viroplasm-like structures in the cytoplasm and recruits viroplasm-associated protein P9-1.Virology journal · 2011Article
- Dual selection mechanisms drive efficient single-gene reverse genetics for rotavirus.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Mechanism of intraparticle synthesis of the rotavirus double-stranded RNA genome.The Journal of biological chemistry · 2010Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Rotavirus NSP2 is an abundant non-structural RNA-binding protein essential for forming the viral factories that support replication of the double-stranded RNA genome. NSP2 exists as stable doughnut-shaped octamers within the infected cell, representing the tail-to-tail interaction of two tetramers. Extending diagonally across the surface of each octamer are four highly basic grooves that function as binding sites for single-stranded RNA. Between the N and C-terminal domains of each monomer is a deep electropositive cleft containing a catalytic site that hydrolyzes the gamma-beta phosphoanhydride bond of any NTP. The catalytic site has similarity to those of the histidine triad (HIT) family of nucleotide-binding proteins. Due to the close proximity of the grooves and clefts, we investigated the possibility that the RNA-binding activity of the groove promoted the insertion of the 5'-triphosphate moiety of the RNA into the cleft, and the subsequent hydrolysis of its gamma-beta phosphoanhydride bond. Our results show that NSP2 hydrolyzes the gammaP from RNAs and NTPs through Mg(2+)-dependent activities that proceed with similar reaction velocities, that require the catalytic His225 residue, and that produce a phosphorylated intermediate. Competition assays indicate that although both substrates enter the active site, RNA is the preferred substrate due to its higher affinity for the octamer. The RNA triphosphatase (RTPase) activity of NSP2 may account for the absence of the 5'-terminal gammaP on the (-) strands of the double-stranded RNA genome segments. This is the first report of a HIT-like protein with a multifunctional catalytic site, capable of accommodating both NTPs and RNAs during gammaP hydrolysis.
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