title: Structural disorder within the replicative complex of measles virus: functional implications.
abstract: Measles virus belongs to the Paramyxoviridae family within the Mononegavirales order. Its non-segmented, single stranded, negative sense RNA genome is encapsidated by the nucleoprotein (N) to form a helical nucleocapsid. This ribonucleoproteic complex is the substrate for both transcription and replication. The RNA-dependent RNA polymerase binds to the nucleocapsid template via its co-factor, the phosphoprotein (P). In this review, we summarize the main experimental data pointing out the abundance of structural disorder within measles virus N and P. We also describe studies indicating that structural disorder is a widespread property in the replicative complex of Paramyxoviridae and, more generally, of Mononegavirales. The functional implications of structural disorder are also discussed. Finally, we propose a model where the flexibility of the disordered N and P domains allows the formation of a tripartite complex (N degrees-P-L) during replication, followed by the delivery of N monomers to the newly synthesized genomic RNA chain.
authors.affiliation: Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS et Universités Aix-Marseille I et II, Campus de Luminy, 13288 Marseille Cedex 09, France.
authors.forename: Jean-Marie
authors.initials: JM
authors.lastname: Bourhis
authors.forename: Bruno
authors.initials: B
authors.lastname: Canard
authors.forename: Sonia
authors.initials: S
authors.lastname: Longhi
mesh_terms: D020816:Amino Acid Motifs; D050884:HSP72 Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D008459:Measles virus / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D008958:Models, Molecular; D018096:Mononegavirales / Q000737:chemistry; D019251:Nucleocapsid / Q000378:metabolism; D019590:Nucleocapsid Proteins; D009698:Nucleoproteins / Q000737:chemistry* / Q000378:metabolism; D018098:Paramyxovirinae / Q000737:chemistry; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D013045:Species Specificity; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism; D014779:Virus Replication
chemical_list: D050884:HSP72 Heat-Shock Proteins; D019590:Nucleocapsid Proteins; D009698:Nucleoproteins; C055859:P protein, Sendai virus; D010750:Phosphoproteins; D014764:Viral Proteins; C058314:nucleoprotein, Measles virus