Next Article in Journal
UPLC–MS Triglyceride Profiling in Sunflower and Rapeseed Seeds
Previous Article in Journal
Total Fatty Acid Analysis of Human Blood Samples in One Minute by High-Resolution Mass Spectrometry
Article Menu

Export Article

Open AccessReview
Biomolecules 2019, 9(1), 8; https://doi.org/10.3390/biom9010008

Modulation of Measles Virus NTAIL Interactions through Fuzziness and Sequence Features of Disordered Binding Sites

1
CNRS and Aix-Marseille Univ Laboratoire Architecture et Fonction des Macromolecules Biologiques (AFMB), UMR 7257 Marseille, France
2
Istituto Pasteur—Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche ‘A. Rossi Fanelli’ and Istituto di Biologia e Patologia Molecolari del Consiglio Nazionale delle Ricerche, Sapienza Università di Roma, 00185 Rome, Italy
*
Authors to whom correspondence should be addressed.
Received: 22 November 2018 / Revised: 10 December 2018 / Accepted: 18 December 2018 / Published: 27 December 2018
(This article belongs to the Special Issue Intrinsically Disordered Proteins and Chronic Diseases)
Full-Text   |   PDF [1427 KB, uploaded 10 January 2019]   |  

Abstract

In this paper we review our recent findings on the different interaction mechanisms of the C-terminal domain of the nucleoprotein (N) of measles virus (MeV) NTAIL, a model viral intrinsically disordered protein (IDP), with two of its known binding partners, i.e., the C-terminal X domain of the phosphoprotein of MeV XD (a globular viral protein) and the heat-shock protein 70 hsp70 (a globular cellular protein). The NTAIL binds both XD and hsp70 via a molecular recognition element (MoRE) that is flanked by two fuzzy regions. The long (85 residues) N-terminal fuzzy region is a natural dampener of the interaction with both XD and hsp70. In the case of binding to XD, the N-terminal fuzzy appendage of NTAIL reduces the rate of α-helical folding of the MoRE. The dampening effect of the fuzzy appendage on XD and hsp70 binding depends on the length and fuzziness of the N-terminal region. Despite this similarity, NTAIL binding to XD and hsp70 appears to rely on completely different requirements. Almost any mutation within the MoRE decreases XD binding, whereas many of them increase the binding to hsp70. In addition, XD binding is very sensitive to the α-helical state of the MoRE, whereas hsp70 is not. Thus, contrary to hsp70, XD binding appears to be strictly dependent on the wild-type primary and secondary structure of the MoRE. View Full-Text
Keywords: IDP; fuzzy interactions; protein complementation assays; split-GFP reassembly; kinetics IDP; fuzzy interactions; protein complementation assays; split-GFP reassembly; kinetics
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Supplementary material

SciFeed

Share & Cite This Article

MDPI and ACS Style

Bignon, C.; Troilo, F.; Gianni, S.; Longhi, S. Modulation of Measles Virus NTAIL Interactions through Fuzziness and Sequence Features of Disordered Binding Sites. Biomolecules 2019, 9, 8.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Biomolecules EISSN 2218-273X Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top