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Article dans une revue

Structural insight into cap-snatching and RNA synthesis by influenza polymerase.

Abstract : Influenza virus polymerase uses a capped primer, derived by 'cap-snatching' from host pre-messenger RNA, to transcribe its RNA genome into mRNA and a stuttering mechanism to generate the poly(A) tail. By contrast, genome replication is unprimed and generates exact full-length copies of the template. Here we use crystal structures of bat influenza A and human influenza B polymerases (FluA and FluB), bound to the viral RNA promoter, to give mechanistic insight into these distinct processes. In the FluA structure, a loop analogous to the priming loop of flavivirus polymerases suggests that influenza could initiate unprimed template replication by a similar mechanism. Comparing the FluA and FluB structures suggests that cap-snatching involves in situ rotation of the PB2 cap-binding domain to direct the capped primer first towards the endonuclease and then into the polymerase active site. The polymerase probably undergoes considerable conformational changes to convert the observed pre-initiation state into the active initiation and elongation states.
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Contributeur : Frank Thomas <>
Soumis le : mardi 17 mars 2015 - 09:03:39
Dernière modification le : lundi 30 septembre 2019 - 10:21:39


  • HAL Id : hal-01132328, version 1
  • PUBMED : 25409151



Stefan Reich, Delphine Guilligay, Alexander Pflug, Hélène Malet, Imre Berger, et al.. Structural insight into cap-snatching and RNA synthesis by influenza polymerase.. Nature, Nature Publishing Group, 2014, 516 (7531), pp.361-6. ⟨hal-01132328⟩



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