In addition to polymerase and cap synthesis activities, replication complexes (RTC) harbor proteases, involved in the maturation of the polyprotein precursors, and RNA processing activities. The latter include helicases that unwind double-stranded RNA structures to favor replication or transcription of the genome. In addition to helicases, we have characterized exonucleases in several virus families. Although the role of these enzymes is still poorly understood, recent studies indicate that these enzymes could be recruited within the replication/transcription complex (RTC) to correct polymerization errors. We are currently characterizing these proof-reading mechanisms for the genus Coronavirus. Finally, we are also interested in the RNA binding properties of the nucleoprotein the Valley Rift nucleoprotein.
- Electrostatic surface potential of the N hexamer
- Mapping of the electrostatic surface potential, from -10 kT in red to +10 kT in blue, onto the surface of hexamer I formed by native N protein reveals a patch of positive charges in the inner part of the ring, which likely accommodates the vRNA. Key residues in the RNA binding site are labeled on the electrostatic surface of a single monomer.