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How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication

Authors
  • Longhi, Sonia1, 2
  • Bloyet, Louis-Marie3, 4, 5, 6, 7
  • Gianni, Stefano8
  • Gerlier, Denis3, 4, 5, 6, 7
  • 1 Aix-Marseille Univ, AFMB UMR 7257, 163, avenue de Luminy, Case 932, Marseille Cedex 09, 13288, France , Marseille Cedex 09 (France)
  • 2 CNRS, AFMB UMR 7257, Marseille, 13288, France , Marseille (France)
  • 3 Université de Lyon, CIRI, International Center for Infectiology Research, Lyon, France , Lyon (France)
  • 4 INSERM, U1111, Lyon, France , Lyon (France)
  • 5 Ecole Normale Supérieure de Lyon, Lyon, France , Lyon (France)
  • 6 Université Claude Bernard Lyon 1, Centre International de Recherche en Infectiologie, Lyon, France , Lyon (France)
  • 7 CNRS, UMR5308, Lyon, France , Lyon (France)
  • 8 Sapienza Università di Roma, Istituto Pasteur, Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche “A. Rossi Fanelli”, Rome, 00185, Italy , Rome (Italy)
Type
Published Article
Journal
Cellular and Molecular Life Sciences
Publisher
Springer-Verlag
Publication Date
Jun 09, 2017
Volume
74
Issue
17
Pages
3091–3118
Identifiers
DOI: 10.1007/s00018-017-2556-3
Source
Springer Nature
Keywords
License
Yellow

Abstract

In this review, we summarize computational and experimental data gathered so far showing that structural disorder is abundant within paramyxoviral nucleoproteins (N) and phosphoproteins (P). In particular, we focus on measles, Nipah, and Hendra viruses and highlight both commonalities and differences with respect to the closely related Sendai virus. The molecular mechanisms that control the disorder-to-order transition undergone by the intrinsically disordered C-terminal domain (NTAIL) of their N proteins upon binding to the C-terminal X domain (XD) of the homologous P proteins are described in detail. By having a significant residual disorder, NTAIL–XD complexes are illustrative examples of “fuzziness”, whose possible functional significance is discussed. Finally, the relevance of N–P interactions as promising targets for innovative antiviral approaches is underscored, and the functional advantages of structural disorder for paramyxoviruses are pinpointed.

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