Structural dissection of human metapneumovirus phosphoprotein using small angle x-ray scattering

Abstract : The phosphoprotein (P) is the main and essential cofactor of the RNA polymerase (L) of non-segmented, negative-strand RNA viruses. P positions the viral polymerase onto its nucleoprotein-RNA template and acts as a chaperone of the nucleoprotein (N), thereby preventing nonspecific encapsidation of cellular RNAs. The phosphoprotein of human metapneumovirus (HMPV) forms homotetramers composed of a stable oligomerization domain (Pcore) flanked by large intrinsically disordered regions (IDRs). Here we combined x-ray crystallography of Pcore with small angle x-ray scattering (SAXS)-based ensemble modeling of the full-length P protein and several of its fragments to provide a structural description of P that captures its dynamic character, and highlights the presence of varyingly stable structural elements within the IDRs. We discuss the implications of the structural properties of HMPV P for the assembly and functioning of the viral transcription/replication machinery.
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https://hal.umontpellier.fr/hal-02075132
Contributeur : Sandrine Beraud <>
Soumis le : jeudi 21 mars 2019 - 11:00:29
Dernière modification le : mardi 28 mai 2019 - 14:12:02

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Max Renner, Guido Paesen, Claire Grison, Sébastien Granier, Jonathan Grimes, et al.. Structural dissection of human metapneumovirus phosphoprotein using small angle x-ray scattering. Scientific Reports, Nature Publishing Group, 2017, 7 (1), pp.14865. ⟨10.1038/s41598-017-14448-z⟩. ⟨hal-02075132⟩

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