tetano
Editor, Senior Moderator
Mol Cell. 2018 May 25. pii: S1097-2765(18)30361-7. doi: 10.1016/j.molcel.2018.05.011. [Epub ahead of print]
[h=1]A Mechanism for the Activation of the Influenza Virus Transcriptase.[/h] Serna Martin I[SUP]1[/SUP], Hengrung N[SUP]2[/SUP], Renner M[SUP]3[/SUP], Sharps J[SUP]1[/SUP], Mart?nez-Alonso M[SUP]1[/SUP], Masiulis S[SUP]3[/SUP], Grimes JM[SUP]4[/SUP], Fodor E[SUP]5[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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[SUB]C[/SUB]) bound to a Ser5-phosphorylated CTD (pS[SUB]5[/SUB]-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[SUB]C[/SUB] are enhanced in the presence of pS[SUB]5[/SUB]-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[SUB]5[/SUB]-CTD of Pol II.
[h=4]KEYWORDS:[/h] CTD; Pol II; RNA polymerase; cap snatching; influenza virus; replication; transcriptase; transcription
PMID: 29910112 DOI: 10.1016/j.molcel.2018.05.011
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[h=1]A Mechanism for the Activation of the Influenza Virus Transcriptase.[/h] Serna Martin I[SUP]1[/SUP], Hengrung N[SUP]2[/SUP], Renner M[SUP]3[/SUP], Sharps J[SUP]1[/SUP], Mart?nez-Alonso M[SUP]1[/SUP], Masiulis S[SUP]3[/SUP], Grimes JM[SUP]4[/SUP], Fodor E[SUP]5[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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[SUB]C[/SUB]) bound to a Ser5-phosphorylated CTD (pS[SUB]5[/SUB]-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[SUB]C[/SUB] are enhanced in the presence of pS[SUB]5[/SUB]-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[SUB]5[/SUB]-CTD of Pol II.
[h=4]KEYWORDS:[/h] CTD; Pol II; RNA polymerase; cap snatching; influenza virus; replication; transcriptase; transcription
PMID: 29910112 DOI: 10.1016/j.molcel.2018.05.011
Free full text