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| Title | A Mechanism for the Activation of the Influenza Virus Transcriptase. |
|---|---|
| Journal, issue, pages | Mol Cell, Vol. 70, Issue 6, Page 1101-11110.e4, Year 2018 |
| Publish date | Jun 21, 2018 |
 Authors | Itziar Serna Martin / Narin Hengrung / Max Renner / Jane Sharps / Mónica Martínez-Alonso / Simonas Masiulis / Jonathan M Grimes / Ervin Fodor /  |
| PubMed Abstract | Influenza virus RNA polymerase (FluPol), a heterotrimer composed of PB1, PB2, and PA subunits (P3 in influenza C), performs both transcription and replication of the viral RNA genome. For ...Influenza virus RNA polymerase (FluPol), a heterotrimer composed of PB1, PB2, and PA subunits (P3 in influenza C), performs both transcription and replication of the viral RNA genome. For transcription, FluPol interacts with the C-terminal domain (CTD) of RNA polymerase II (Pol II), which enables FluPol to snatch capped RNA primers from nascent host RNAs. Here, we describe the co-crystal structure of influenza C virus polymerase (FluPol) bound to a Ser5-phosphorylated CTD (pS-CTD) peptide. The position of the CTD-binding site at the interface of PB1, P3, and the flexible PB2 C-terminal domains suggests that CTD binding stabilizes the transcription-competent conformation of FluPol. In agreement, both cap snatching and capped primer-dependent transcription initiation by FluPol are enhanced in the presence of pS-CTD. Mutations of amino acids in the CTD-binding site reduce viral mRNA synthesis. We propose a model for the activation of the influenza virus transcriptase through its association with pS-CTD of Pol II. |
 External links | Mol Cell / PubMed:29910112 / PubMed Central |
| Methods | EM (single particle) / X-ray diffraction |
| Resolution | 4.14 - 9.8 Å |
| Structure data | EMDB-4190, PDB-6f5o:  PDB-6f5p: |
| Chemicals |  ChemComp-MG: |
| Source |
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 Keywords |  VIRAL PROTEIN / influenza virus RNA dependent RNA polymerase / REPLICATION / influenza virus RNA polymerase / Pol II / transcription |
fopius arisanus (insect)
