title: Influenza virus inhibits RNA polymerase II elongation.
abstract: The influenza virus RNA-dependent RNA polymerase interacts with the serine-5 phosphorylated carboxy-terminal domain (CTD) of the large subunit of RNA polymerase II (Pol II). It was proposed that this interaction allows the viral RNA polymerase to gain access to host mRNA-derived capped RNA fragments required as primers for the initiation of viral mRNA synthesis. Here, we show, using a chromatin immunoprecipitation (ChIP) analysis, that similar amounts of Pol II associate with Pol II promoter DNAs in influenza virus-infected and mock-infected cells. However, there is a statistically significant reduction in Pol II densities in the coding region of Pol II genes in infected cells. Thus, influenza virus specifically interferes with Pol II elongation, but not Pol II initiation. We propose that influenza virus RNA polymerase, by binding to the CTD of initiating Pol II and subsequent cleavage of the capped 5' end of the nascent transcript, triggers premature Pol II termination.
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
authors.forename: Annie Y
authors.initials: AY
authors.lastname: Chan
authors.forename: Frank T
authors.initials: FT
authors.lastname: Vreede
authors.forename: Matt
authors.initials: M
authors.lastname: Smith
authors.forename: Othmar G
authors.initials: OG
authors.lastname: Engelhardt
authors.forename: Ervin
authors.initials: E
authors.lastname: Fodor
mesh_terms: D047369:Chromatin Immunoprecipitation; D006367:HeLa Cells; D006801:Humans; D009980:Influenza A virus / Q000201:enzymology / Q000502:physiology*; D011485:Protein Binding; D012319:RNA Polymerase II / Q000378:metabolism*; D012324:RNA-Dependent RNA Polymerase / Q000378:metabolism; D014158:Transcription, Genetic
chemical_list: D012319:RNA Polymerase II; D012324:RNA-Dependent RNA Polymerase