RNA-free and ribonucleoprotein-associated influenza virus polymerases directly bind the serine-5 phosphorylated carboxyl-terminal domain of host RNA polymerase IIReport as inadecuate




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Reference: Fodor, E, Hengrung, N and Martinez-Alonso, M, (2016). 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.Citable link to this page:

 

RNA-free and ribonucleoprotein-associated influenza virus polymerases directly bind the serine-5 phosphorylated carboxyl-terminal domain of host RNA polymerase II

Abstract: Influenza viruses subvert the transcriptional machinery of their hosts to synthesise their own viral mRNA. Ongoing transcription by cellular RNA polymerase II (Pol II) is required for viral mRNA synthesis. By a process known as cap-snatching, the virus steals short 5ʹ capped RNA fragments from host capped RNAs and uses these to prime viral transcription. An interaction between the influenza A virus RNA polymerase and the C-terminal domain (CTD) of the large subunit of Pol II has been established, but the molecular details of this interaction remain unknown. We show here that influenza virus ribonucleoprotein (vRNP) complex binds to the CTD of transcriptionally engaged Pol II. Furthermore, we provide evidence that the viral polymerase binds directly to the serine-5 phosphorylated form of the Pol II CTD, both in the presence and absence of viral RNA, and show that this interaction is conserved in evolutionarily distant influenza viruses. We propose a model in which direct binding of the viral RNA polymerase in the context of vRNPs to Pol II early in infection facilitates cap-snatching, while we suggest that binding of free viral polymerase to Pol II late in infection may trigger Pol II degradation.

Peer Review status:Peer reviewedPublication status:PublishedVersion:Publisher's versionNotes:Copyright © 2016 Martinez-Alonso et al. All Rights Reserved. This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license. This is the author accepted manuscript following peer review version of the article. The final version may be available online from American Society For Microbiology at: https://doi.org/10.1128/JVI.00494-16

Bibliographic Details

Publisher: American Society for Microbiology

Publisher Website: http://www.asm.org/

Publisher: American Society for Microbiology

Journal: Journal of Virologysee more from them

Publication Website: http://jvi.asm.org/

Issue Date: 2016-04-20Identifiers

Urn: uuid:366ad87c-1765-4616-812c-0725718ffd9a

Source identifier: 616079

Eissn: 1098-5514

Doi: https://doi.org/10.1128/JVI.00494-16

Issn: 0022-538X Item Description

Type: Journal article;

Version: Publisher's version Tiny URL: pubs:616079

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Author: Fodor, E - institutionUniversity of Oxford Oxford, MSD, Pathology Dunn School grantNumberMR-K000241-1 fundingMedical Research Cou

Source: https://ora.ox.ac.uk/objects/uuid:366ad87c-1765-4616-812c-0725718ffd9a



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