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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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Modulation of Measles Virus NTAIL Interactions through Fuzziness and Sequence Features of Disordered Binding Sites

Christophe Bignon1, Francesca Troilo2,3, Stefano Gianni4

  • 1CNRS and Aix-Marseille Univ Laboratoire Architecture et Fonction des Macromolecules Biologiques (AFMB), UMR 7257 Marseille, France. christophe.bignon@afmb.univ-mrs.fr.

Biomolecules
|December 29, 2018
PubMed

Insights

Measles virus nucleoprotein (NTAIL) interactions with viral XD and cellular hsp70 differ significantly. While both bind via a molecular recognition element (MoRE), NTAIL

Area of Science:

  • Structural biology
  • Virology
  • Protein-protein interactions

Background:

  • Measles virus nucleoprotein (NTAIL) is an intrinsically disordered protein (IDP) model.
  • NTAIL interacts with viral phosphoprotein's C-terminal X domain (XD) and cellular heat-shock protein 70 (hsp70).
  • These interactions involve a molecular recognition element (MoRE) flanked by disordered 'fuzzy' regions.

Purpose of the Study:

  • To investigate the distinct interaction mechanisms of NTAIL with XD and hsp70.
  • To elucidate the role of intrinsically disordered regions in modulating protein binding.
  • To compare the structural requirements for binding to a viral protein (XD) versus a cellular protein (hsp70).

Main Methods:

  • Analysis of interaction mechanisms between NTAIL, XD, and hsp70.
  • Investigating the influence of mutations within the MoRE on binding affinities.
  • Assessing the sensitivity of binding to the secondary structure of the MoRE.

Main Results:

  • The N-terminal fuzzy region of NTAIL acts as a dampener for both XD and hsp70 interactions.
  • Mutations in the MoRE negatively impact XD binding but often enhance hsp70 binding.
  • XD binding is highly dependent on the MoRE's α-helical state, unlike hsp70 binding.

Conclusions:

  • Despite shared binding elements, NTAIL interactions with XD and hsp70 are regulated by different mechanisms.
  • The disordered N-terminal region plays a crucial role in modulating binding affinity and specificity.
  • XD binding requires specific primary and secondary structures, while hsp70 binding is more flexible.
Keywords:
IDPfuzzy interactionskineticsprotein complementation assayssplit-GFP reassembly

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