ArticleJournal of virology2001
Identification and characterization of the helix-destabilizing activity of rotavirus nonstructural protein NSP2.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
42 citing papers in PubMed, 92 citations in OpenAlex.
- Review
- Review
- Cryo-EM structure of rotavirus B NSP2 reveals its unique tertiary architecture.Journal of virology · 2024Article
- Flexibility of the Rotavirus NSP2 C-Terminal Region Supports Factory Formation via Liquid-Liquid Phase Separation.Journal of virology · 2023Article
- Rotavirus RNA chaperone mediates global transcriptome-wide increase in RNA backbone flexibility.Nucleic acids research · 2022Article
- Structural basis of rotavirus RNA chaperone displacement and RNA annealing.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- Understanding the penetrance of intrinsic protein disorder in rotavirus proteome.International journal of biological macromolecules · 2020Article
- Protein-mediated RNA folding governs sequence-specific interactions between rotavirus genome segments.eLife · 2017Article
- RNA chaperones encoded by RNA viruses.Virologica Sinica · 2015Review
- Evidence that avian reovirus σNS is an RNA chaperone: implications for genome segment assortment.Nucleic acids research · 2015Article
- Article
- Probing the sites of interactions of rotaviral proteins involved in replication.Journal of virology · 2014Article
- A cypovirus VP5 displays the RNA chaperone-like activity that destabilizes RNA helices and accelerates strand annealing.Nucleic acids research · 2014Article
- Further characterisation of rotavirus cores: Ss(+)RNAs can be packaged in vitro but packaging lacks sequence specificity.Virus research · 2013Article
- The nonstructural protein 2C of a Picorna-like virus displays nucleic acid helix destabilizing activity that can be functionally separated from its ATPase activity.Journal of virology · 2013Article
- Minimum requirements for bluetongue virus primary replication in vivo.Journal of virology · 2013Article
- Molecular characterization of the porcine group A rotavirus NSP2 and NSP5/6 genes from São Paulo State, Brazil, in 2011/12.TheScientificWorldJournal · 2013Article
- 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
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The rotavirus nonstructural protein NSP2 self-assembles into homomultimers, binds single-stranded RNA nonspecifically, possesses a Mg2+-dependent nucleoside triphosphatase (NTPase) activity, and is a component of replication intermediates. Because these properties are characteristics of known viral helicases, we examined the possibility that this was also an activity of NSP2 by using a strand displacement assay and purified bacterially expressed protein. The results revealed that, under saturating concentrations, NSP2 disrupted both DNA-RNA and RNA-RNA duplexes; hence, the protein possesses helix-destabilizing activity. However, unlike typical helicases, NSP2 required neither a divalent cation nor a nucleotide energy source for helix destabilization. Further characterization showed that NSP2 displayed no polarity in destabilizing a partial duplex. In addition, helix destabilization by NSP2 was found to proceed cooperatively and rapidly. The presence of Mg2+ and other divalent cations inhibited by approximately one-half the activity of NSP2, probably due to the increased stability of the duplex substrate brought on by the cations. In contrast, under conditions where NSP2 functions as an NTPase, its helix-destabilizing activity was less sensitive to the presence of Mg2+, suggesting that in the cellular environment the two activities associated with the protein, helix destabilization and NTPase, may function together. Although distinct from typical helicases, the helix-destabilizing activity of NSP2 is quite similar to that of the sigmaNS protein of reovirus and to the single-stranded DNA-binding proteins (SSBs) involved in double-stranded DNA replication. The presence of SSB-like nonstructural proteins in two members of the family Reoviridae suggests a common mechanism of unwinding viral mRNA prior to packaging and subsequent minus-strand RNA synthesis.
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