Ordre et désordre au sein du complexe réplicatif des paramyxovirus

In the last decade there has been an increasing amount of experimental and computational evidence pointing out that the proteome of eukaryotes and viruses is enriched in intrinsically disordered protein (IDPs) and/or intrinsically disordered regions (IDRs). IDPs/IDRs are ubiquitous functional proteins that lack stable II and III structures under physiological conditions in the absence of a partner and that rather exist as highly dynamic conformational ensembles. IDPs are often involved in biological processes implying manifold protein-protein interactions, such as cellular regulation, transcription and signal transduction.
In the course of the structural and functional characterization of the measles virus replicative complex, we discovered that the nucleoprotein (N) and the phosphoprotein (P) contain long (up to 230 residues) disordered regions possessing sequence and biochemical features that typify IDPs. More recently, by combining computational and experimental approaches, we extended these results to the N and P proteins from the newly emerged Nipah and Hendra viruses. My talk will focus on (i) the identification and characterization of disordered regions of the N and P proteins of these paramyxoviruses, (ii) the assessment of their structural state in the context of the full-length N and P proteins, (iii) the investigation of the molecular mechanisms underlying the induced folding events triggered by binding partners. Finally, the functional implications of disorder within the replicative complex of these viruses will be discussed. 

 More info:
 http://www.afmb.univ-mrs.fr/desordre-structural