Structural disorder and modular organization in Paramyxovirinae N and P

David Karlin1, François Ferron1, Bruno Canard1

  • 1Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS et Université Aix-Marseille I et II, ESIL, Campus de Luminy, 13288 Marseille Cedex 09, France.

Insights

Paramyxovirinae viruses possess intrinsically disordered proteins crucial for replication. This widespread disorder in nucleoprotein (N) and phosphoprotein (P) underlies their function and interactions.

Area of Science:

  • Molecular Biology
  • Virology
  • Structural Biology

Background:

  • The replicative complex of Paramyxovirinae, including nucleoprotein (N), phosphoprotein (P), and polymerase (L), is essential for viral function.
  • Previous studies indicated intrinsic disorder in specific domains of measles virus N and P proteins.

Purpose of the Study:

  • To investigate the extent and significance of intrinsic disorder within the Paramyxovirinae replicative complex.
  • To identify conserved organizational principles and functional roles of disordered regions in N and P proteins.

Main Methods:

  • Employed a combination of computational approaches based on diverse physico-chemical principles to predict intrinsic disorder.
  • Conducted a thorough literature review to gather experimental evidence supporting computational predictions.

Main Results:

  • Intrinsic disorder is a prevalent characteristic of Paramyxovirinae N and P proteins.
  • Identified a conserved modular organization in Paramyxovirinae P proteins, comprising six modules based on structural or sequence conservation.
  • Unstructured regions of N and P proteins are implicated in multiple interactions with protein and protein-RNA partners.

Conclusions:

  • Intrinsic disorder plays a significant role in the function and interactions of the Paramyxovirinae replicative complex.
  • This study contributes to understanding intrinsically disordered proteins and aids in identifying target domains for future structural studies.

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