A Mechanism for the Activation of the Influenza Virus Transcriptase.

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 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_C) bound to a Ser5-phosphorylated CTD (pS₅-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

SUBMITTER: Serna Martin I 

PROVIDER: S-EPMC6024077 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature