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Article: The RNA polymerase of influenza virus, bound to the 5' end of virion RNA, acts in cis to polyadenylate mRNA

TitleThe RNA polymerase of influenza virus, bound to the 5' end of virion RNA, acts in cis to polyadenylate mRNA
Authors
Issue Date1998
PublisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/
Citation
Journal Of Virology, 1998, v. 72 n. 10, p. 8214-8219 How to Cite?
AbstractWe previously demonstrated, by limited mutagenesis, that conserved sequence elements within the 5' end of influenza virus virion RNA (vRNA) are required for the polyadenylation of mRNA in vitro. To further characterize the nucleotide residues at the 5' end of vRNA which might be involved in polyadenylation, a complete set of short and long model vRNA-like templates with mutations at nucleotides 1' to 13' (prime notation denotes numbering from the 5' end) of vRNA were synthesized and transcribed in vitro. The products were assayed for mRNA production with both reverse transcription- PCR and [α-32P]ATP incorporation assays. Results from these independent assays showed that vRNA templates with point mutations at positions 2', 3', 7' to 9', and 11' to 13' synthesized polyadenylated transcripts inefficiently compared with those with mutations at positions 1', 4' to 6', and 10'. Positions 2', 3', 7' to 9', and 11' are known to be involved in RNA polymerase binding. Furthermore, residues at positions 11' to 13' are known to be involved in base pairing between the 3' and 5' ends of vRNA. These findings demonstrate that the RNA polymerase has to bind to the 5' end of the template vRNA, which must then interact with the 3' end of the same template for polyadenylation to occur. These results support a model in which a cis- acting RNA polymerase is required for the polyadenylation of influenza virus.
Persistent Identifierhttp://hdl.handle.net/10722/179759
ISSN
2015 Impact Factor: 4.606
2015 SCImago Journal Rankings: 3.347
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorPoon, LLMen_US
dc.contributor.authorPritlove, DCen_US
dc.contributor.authorSharps, Jen_US
dc.contributor.authorBrownlee, GGen_US
dc.date.accessioned2012-12-19T10:04:22Z-
dc.date.available2012-12-19T10:04:22Z-
dc.date.issued1998en_US
dc.identifier.citationJournal Of Virology, 1998, v. 72 n. 10, p. 8214-8219en_US
dc.identifier.issn0022-538Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/179759-
dc.description.abstractWe previously demonstrated, by limited mutagenesis, that conserved sequence elements within the 5' end of influenza virus virion RNA (vRNA) are required for the polyadenylation of mRNA in vitro. To further characterize the nucleotide residues at the 5' end of vRNA which might be involved in polyadenylation, a complete set of short and long model vRNA-like templates with mutations at nucleotides 1' to 13' (prime notation denotes numbering from the 5' end) of vRNA were synthesized and transcribed in vitro. The products were assayed for mRNA production with both reverse transcription- PCR and [α-32P]ATP incorporation assays. Results from these independent assays showed that vRNA templates with point mutations at positions 2', 3', 7' to 9', and 11' to 13' synthesized polyadenylated transcripts inefficiently compared with those with mutations at positions 1', 4' to 6', and 10'. Positions 2', 3', 7' to 9', and 11' are known to be involved in RNA polymerase binding. Furthermore, residues at positions 11' to 13' are known to be involved in base pairing between the 3' and 5' ends of vRNA. These findings demonstrate that the RNA polymerase has to bind to the 5' end of the template vRNA, which must then interact with the 3' end of the same template for polyadenylation to occur. These results support a model in which a cis- acting RNA polymerase is required for the polyadenylation of influenza virus.en_US
dc.languageengen_US
dc.publisherAmerican Society for Microbiology. The Journal's web site is located at http://jvi.asm.org/en_US
dc.relation.ispartofJournal of Virologyen_US
dc.subject.meshAdenosine Triphosphate - Metabolismen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshDna-Directed Rna Polymerases - Metabolismen_US
dc.subject.meshInfluenza A Virus - Enzymologyen_US
dc.subject.meshNucleic Acid Conformationen_US
dc.subject.meshPhosphorus Radioisotopesen_US
dc.subject.meshPoint Mutationen_US
dc.subject.meshPolymerase Chain Reactionen_US
dc.subject.meshRna, Messenger - Chemistry - Metabolismen_US
dc.subject.meshRna, Viral - Chemistry - Metabolismen_US
dc.titleThe RNA polymerase of influenza virus, bound to the 5' end of virion RNA, acts in cis to polyadenylate mRNAen_US
dc.typeArticleen_US
dc.identifier.emailPoon, LLM: llmpoon@hkucc.hku.hken_US
dc.identifier.authorityPoon, LLM=rp00484en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid9733864-
dc.identifier.scopuseid_2-s2.0-0031667216en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0031667216&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume72en_US
dc.identifier.issue10en_US
dc.identifier.spage8214en_US
dc.identifier.epage8219en_US
dc.identifier.isiWOS:000075864100059-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridPoon, LLM=7005441747en_US
dc.identifier.scopusauthoridPritlove, DC=6602418386en_US
dc.identifier.scopusauthoridSharps, J=6602899431en_US
dc.identifier.scopusauthoridBrownlee, GG=35994351900en_US

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