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Article dans une revue

The Nucleoprotein and Phosphoprotein of Measles Virus

Abstract : Measles virus is a negative strand virus and the genomic and antigenomic RNA binds to the nucleoprotein (N), assembling into a helical nucleocapsid. The polymerase complex comprises two proteins, the Large protein (L), that both polymerizes RNA and caps the mRNA, and the phosphoprotein (P) that co-localizes with L on the nucleocapsid. This review presents recent results about N and P, in particular concerning their intrinsically disordered domains. N is a protein of 525 residues with a 120 amino acid disordered C-terminal domain, Ntail. The first 50 residues of Ntail extricate the disordered chain from the nucleocapsid, thereby loosening the otherwise rigid structure, and the C-terminus contains a linear motif that binds P. Recent results show how the 5' end of the viral RNA binds to N within the nucleocapsid and also show that the bases at the 3' end of the RNA are rather accessible to the viral polymerase. P is a tetramer and most of the protein is disordered; comprising 507 residues of which around 380 are disordered. The first 37 residues of P bind N, chaperoning against non-specific interaction with cellular RNA, while a second interaction site, around residue 200 also binds N. In addition, there is another interaction between C-terminal domain of P (XD) and Ntail. These results allow us to propose a new model of how the polymerase binds to the nucleocapsid and suggests a mechanism for initiation of transcription.
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https://hal.univ-grenoble-alpes.fr/hal-02383245
Contributeur : Frank Thomas <>
Soumis le : mercredi 27 novembre 2019 - 16:09:25
Dernière modification le : mardi 6 octobre 2020 - 16:12:09

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Serafima Guseva, Sigrid Milles, Martin Blackledge, Rob W H Ruigrok. The Nucleoprotein and Phosphoprotein of Measles Virus. Frontiers in Microbiology, Frontiers Media, 2019, 10 (1832), pp.1-10. ⟨10.3389/fmicb.2019.01832⟩. ⟨hal-02383245⟩

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