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Identification of novel amino acid residues of influenza virus PA-X that are important for PA-X shutoff activity by using yeast

tetano

Editor, Senior Moderator
Virology. 2018 Jan 10;516:71-75. doi: 10.1016/j.virol.2018.01.004. [Epub ahead of print]
[h=1]Identification of novel amino acid residues of influenza virus PA-X that are important for PA-X shutoff activity by using yeast.[/h] Oishi K[SUP]1[/SUP], Yamayoshi S[SUP]2[/SUP], Kawaoka Y[SUP]3[/SUP].
[h=3]Author information[/h]

[h=3]Abstract[/h] The influenza A virus protein PA-X comprises an N-terminal PA region and a C-terminal PA-X-specific region. PA-X suppresses host gene expression, termed shutoff, via mRNA cleavage. Although the endonuclease active site in the N-terminal PA region of PA-X and basic amino acids in the C-terminal PA-X-specific region are known to be important for PA-X shutoff activity, other amino acids may also play a role. Here, we used yeast to identify novel amino acids of PA-X that are important for PA-X shutoff activity. Unlike wild-type PA-X, most PA-X mutants predominantly localized in the cytoplasm, indicating that these mutations decreased the shutoff activity of PA-X by affecting PA-X translocation to the nucleus. Mapping of the identified amino acids onto the N-terminal structure of PA revealed that some of them likely contribute to the formation of the endonuclease active site of PA.


[h=4]KEYWORDS:[/h] Influenza; PA-X; Shutoff; Yeasts

PMID: 29331676 DOI: 10.1016/j.virol.2018.01.004
 
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