ArticleJournal of virology2002
The RNA polymerase of influenza a virus is stabilized by interaction with its viral RNA promoter.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 71 citations in OpenAlex.
- Identification of a Type-Specific Promoter Element That Differentiates between Influenza A and B Viruses.Journal of virology · 2019Article
- Focusing on the Influenza Virus Polymerase Complex: Recent Progress in Drug Discovery and Assay Development.Current medicinal chemistry · 2019Review
- Single-molecule fluorescence imaging: Generating insights into molecular interactions in virology.Journal of biosciences · 2018Review
- Article
- RNA-Free and Ribonucleoprotein-Associated Influenza Virus Polymerases Directly Bind the Serine-5-Phosphorylated Carboxyl-Terminal Domain of Host RNA Polymerase II.Journal of virology · 2016Article
- Recent Advances in Developing Small Molecules Targeting Nucleic Acid.International journal of molecular sciences · 2016Review
- Structural characterization of recombinant IAV polymerase reveals a stable complex between viral PA-PB1 heterodimer and host RanBP5.Scientific reports · 2016Article
- Influenza virus activation of the interferon system.Virus research · 2015Review
- DnaJA1/Hsp40 is co-opted by influenza A virus to enhance its viral RNA polymerase activity.Journal of virology · 2014Article
- Interactome analysis of the influenza A virus transcription/replication machinery identifies protein phosphatase 6 as a cellular factor required for efficient virus replication.Journal of virology · 2014Article
- The RNA-dependent RNA polymerase of the influenza A virus.Future virology · 2014Article
- Single-molecule FRET reveals a corkscrew RNA structure for the polymerase-bound influenza virus promoter.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Activation of the interferon induction cascade by influenza a viruses requires viral RNA synthesis and nuclear export.Journal of virology · 2014Article
- A novel small-molecule binds to the influenza A virus RNA promoter and inhibits viral replication.Chemical communications (Cambridge, England) · 2014Article
- Identification of conserved RNA secondary structures at influenza B and C splice sites reveals similarities and differences between influenza A, B, and C.BMC research notes · 2014Article
- Impact of the segment-specific region of the 3'-untranslated region of the influenza A virus PB1 segment on protein expression.Virus genes · 2013Article
- Isolation and characterization of the positive-sense replicative intermediate of a negative-strand RNA virus.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- Cellular protein HAX1 interacts with the influenza A virus PA polymerase subunit and impedes its nuclear translocation.Journal of virology · 2013Article
- A small-RNA enhancer of viral polymerase activity.Journal of virology · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RNA polymerase of the influenza virus is responsible for the transcription and replication of the segmented RNA viral genome during infection of host cells. Polymerase function is known to be strictly dependent on interaction with its RNA promoter, but no attempts to investigate whether the virion RNA (vRNA) promoter stabilizes the polymerase have been reported previously. Here we tested whether the vRNA promoter protects the polymerase against heat inactivation. We prepared partially purified recombinant influenza A virus RNA polymerase, in the absence of influenza virus vRNA promoter sequences, by transient transfection of expression plasmids into human kidney 293T cells. The polymerase was found to be heat labile at 40 degrees C in the absence of added vRNA. However, it was protected from heat inactivation if both the 5' and 3' strands of the vRNA promoter were present. By using the ability of vRNA to protect the enzyme against heat inactivation, we established a novel assay, in conjunction with a mutagenic approach, that was used to test the secondary structure requirement of the vRNA promoter for polymerase binding. Binding required a panhandle structure and the presence of local hairpin loop structures in both the 5' and 3' ends of vRNA, as suggested by the corkscrew model. The interaction of the vRNA promoter with the influenza virus RNA polymerase heterotrimeric complex is likely to favor a particular closed conformation of the complex, thereby ensuring the stability of the RNA polymerase within both the infected cell and the isolated virus.
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Registered trials
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.