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Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes

Abstract : Bunyavirales is an order of segmented negative-strand RNA viruses comprising several life-threatening pathogens against which no effective treatment is currently available. Replication and transcription of the RNA genome constitute essential processes performed by the virally encoded multi-domain RNA-dependent RNA polymerase. Here, we describe the complete high-resolution cryo-EM structure of La Crosse virus polymerase. It reveals the presence of key protruding C-terminal domains, notably the cap-binding domain, which undergoes large movements related to its role in transcription initiation, and a zinc-binding domain that displays a fold not previously observed. We capture the polymerase structure at pre-initiation and elongation states, uncovering the coordinated movement of the priming loop, mid-thumb ring linker and lid domain required for the establishment of a ten-base-pair template-product RNA duplex before strand separation into respective exit tunnels. These structural details and the observed dynamics of key functional elements will be instrumental for structure-based development of polymerase inhibitors.
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https://hal.univ-grenoble-alpes.fr/hal-02907948
Contributeur : Frank Thomas <>
Soumis le : mardi 28 juillet 2020 - 08:23:48
Dernière modification le : vendredi 31 juillet 2020 - 03:12:35

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Benoît Arragain, Grégory Effantin, Piotr Gerlach, Juan Reguera, Guy Schoehn, et al.. Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes. Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.3590. ⟨10.1038/s41467-020-17349-4⟩. ⟨hal-02907948⟩

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