tetano
Editor, Senior Moderator
J Gen Virol. 2017 May 22. doi: 10.1099/jgv.0.000750. [Epub ahead of print]
[h=1]Basic amino acids in the N-terminal half of the PB2 subunit of influenza virus RNA polymerase are involved in both transcription and replication.[/h] Hara K[SUP]1[/SUP], Kashiwagi T[SUP]1[/SUP], Hamada N[SUP]1[/SUP], Watanabe H[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The PB2 subunit of influenza virus RNA polymerase is known to be involved in the initiation of transcription of the virus genome via cap binding. However, other specific roles of PB2 for viral RNA synthesis are not well understood. Here, we demonstrate that basic residues, 124R, 142R, 143R, 268R and 331K/332R, in the N-terminal half of PB2 are important for the polymerase activity. Notably, R124A mutation remarkably reduced the synthesis of mRNA, cRNA and vRNA in vivo, which was in good agreement with the data obtained in vitro. Cross-linking studies suggested that a reduction of the polymerase activity in the R124A mutant was due to a significant decrease in binding to the viral RNA promoter. In the three-dimensional structure of the polymerase, 124R is visible through the NTP tunnel and is located close to the polymerase active site. We propose that 124R plays a key role in promoter binding during RNA synthesis.
PMID: 28530165 DOI: 10.1099/jgv.0.000750
[h=1]Basic amino acids in the N-terminal half of the PB2 subunit of influenza virus RNA polymerase are involved in both transcription and replication.[/h] Hara K[SUP]1[/SUP], Kashiwagi T[SUP]1[/SUP], Hamada N[SUP]1[/SUP], Watanabe H[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The PB2 subunit of influenza virus RNA polymerase is known to be involved in the initiation of transcription of the virus genome via cap binding. However, other specific roles of PB2 for viral RNA synthesis are not well understood. Here, we demonstrate that basic residues, 124R, 142R, 143R, 268R and 331K/332R, in the N-terminal half of PB2 are important for the polymerase activity. Notably, R124A mutation remarkably reduced the synthesis of mRNA, cRNA and vRNA in vivo, which was in good agreement with the data obtained in vitro. Cross-linking studies suggested that a reduction of the polymerase activity in the R124A mutant was due to a significant decrease in binding to the viral RNA promoter. In the three-dimensional structure of the polymerase, 124R is visible through the NTP tunnel and is located close to the polymerase active site. We propose that 124R plays a key role in promoter binding during RNA synthesis.
PMID: 28530165 DOI: 10.1099/jgv.0.000750