ArticleThe EMBO journal2001
The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
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Who cites it
79 citing papers in PubMed, 198 citations in OpenAlex.
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- Investigation of Binding Affinity between Potential Antiviral Agents and PB2 Protein of Influenza A: Non-equilibrium Molecular Dynamics Simulation Approach.International journal of medical sciences · 2020Article
- Inventory of molecular markers affecting biological characteristics of avian influenza A viruses.Virus genes · 2019Review
- Evolution of Therapeutic Antibodies, Influenza Virus Biology, Influenza, and Influenza Immunotherapy.BioMed research international · 2018Review
- Molecular characterization of emaraviruses associated with Pigeonpea sterility mosaic disease.Scientific reports · 2017Article
- Identification of influenza A nucleoprotein body domain residues essential for viral RNA expression expose antiviral target.Virology journal · 2017Article
- The Influenza Virus Polymerase Complex: An Update on Its Structure, Functions, and Significance for Antiviral Drug Design.Medicinal research reviews · 2016Review
- Inhibition of endosomal fusion activity of influenza virus by Rheum tanguticum (da-huang).Scientific reports · 2016Article
- Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains.Molecular cell · 2016Article
- Functional Constraint Profiling of a Viral Protein Reveals Discordance of Evolutionary Conservation and Functionality.PLoS genetics · 2015Article
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- Common and unique features of viral RNA-dependent polymerases.Cellular and molecular life sciences : CMLS · 2014Review
19 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
The cap-dependent endonuclease of the influenza viral RNA polymerase, which produces the capped RNA primers that initiate viral mRNA synthesis, is comprised of two active sites, one for cap binding and one for endonuclease cleavage. We identify the amino acid sequences that constitute these two active sites and demonstrate that they are located on different polymerase subunits. Binding of the 5' terminal sequence of virion RNA (vRNA) to the polymerase activates a tryptophan-rich, cap-binding sequence on the PB2 subunit. At least one of the tryptophans functions in cap binding, indicating that this active site is probably similar to that of other known cap-binding proteins. Endonuclease cleavage, which is activated by the subsequent binding of the 3' terminal sequence of vRNA, resides in a PB1 sequence that contains three essential acidic amino acids, similar to the active sites of other enzymes that cut polynucleotides to produce 3'-OH ends. These results, coupled with those of our previous study, provide a molecular map of the five known essential active sites of the influenza viral polymerase.
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