Experimental Characterization of Fuzzy Protein Assemblies: Interactions of Paramyxoviral NTAIL Domains With Their Functional Partners

Francesca Troilo, Christophe Bignon, Stefano Gianni, Monika Fuxreiter, Sonia Longhi

Research output: Chapter in Book/Report/Conference proceedingChapter

5 Citations (Scopus)

Abstract

In this chapter we detail various experimental approaches to characterize the fuzziness of complexes made of the C-terminal domain of the nucleoprotein (NTAIL) from three representative paramyxoviruses and of the C-terminal X domain (XD) of the homologous phosphoprotein. We discuss the advantages, the limitations, as well as the caveats of the various methods. We describe experimental data showing that paramyxoviral NTAIL–XD complexes are characterized by a considerable amount of conformational heterogeneity. We also detail recent data that revealed that NTAIL is highly malleable, i.e., it displays a partner-mediated polymorphism. All the results suggest that NTAIL plasticity and fuzziness play a role in the coordination and regulation of the NTAIL interaction network so as to ensure efficient transcription and replication.

Original languageEnglish
Title of host publicationMethods in Enzymology
EditorsElizabeth Rhoades
PublisherAcademic Press Inc.
Pages137-192
Number of pages56
ISBN (Print)9780128156490
DOIs
Publication statusPublished - 2018

Publication series

NameMethods in Enzymology
Volume611
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

Keywords

  • ESI-MS and IM-MS
  • Experimental assessment of fuzziness
  • Fuzzy interactions
  • Impact of fuzziness on binding
  • Kinetics
  • Mutagenesis
  • NMR
  • Protein complementation assays
  • SAXS
  • SEC
  • Site-directed spin-labeling EPR spectroscopy
  • Split-GFP reassembly

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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    Troilo, F., Bignon, C., Gianni, S., Fuxreiter, M., & Longhi, S. (2018). Experimental Characterization of Fuzzy Protein Assemblies: Interactions of Paramyxoviral NTAIL Domains With Their Functional Partners. In E. Rhoades (Ed.), Methods in Enzymology (pp. 137-192). (Methods in Enzymology; Vol. 611). Academic Press Inc.. https://doi.org/10.1016/bs.mie.2018.08.006