{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Serna Martin I"],"funding":["Medical Research Council","Seventh Framework Programme","Wellcome Trust"],"pagination":["1101-1110.e4"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6024077"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["70(6)"],"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 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 "],"journal":["Molecular cell"],"pubmed_title":["A Mechanism for the Activation of the Influenza Virus Transcriptase."],"pmcid":["PMC6024077"],"funding_grant_id":["203141/Z/16/Z","MR/R009945/1","1374922","084655/Z/08/Z","200835/Z/16/Z","092931/Z/10/Z","204703/Z/16/Z","PIEF-GA-2012-328746","MR/K000241/1"],"pubmed_authors":["Fodor E","Martinez-Alonso M","Renner M","Grimes JM","Hengrung N","Sharps J","Masiulis S","Serna Martin I"],"additional_accession":[]},"is_claimable":false,"name":"A Mechanism for the Activation of the Influenza Virus Transcriptase.","description":"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 ","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Jun","modification":"2026-04-30T21:44:08.353Z","creation":"2019-03-26T23:44:43Z"},"accession":"S-EPMC6024077","cross_references":{"pubmed":["29910112"],"doi":["10.1016/j.molcel.2018.05.011"]}}