Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR

Bernard, Cedric; Gely, Stéphane; Bourhis, Jean-Marie; Morelli, Xavier; Longhi, Sonia; Darbon, Hervé

doi:10.1016/j.febslet.2009.03.004

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Volume 583, Issue 7 , Pages 1084-1089, 2 April 2009

Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR

Edited by Gianni Cesareni

Cedric Bernard
- Architecture et Fonction des Macromolécules Biologiques, UMR6098, CNRS, Université de Provence et Université de la Méditerranée, case 932, 163 Avenue de Luminy, 13288 Marseille Cedex 9, France
- Corresponding authors. Address: AFMB-UMR 6098, CNRS et Universités d’Aix-Marseille I and II, 163 avenue de Luminy, Case 932, 13288 Marseille Cedex 09. Fax: +33(0)491266720.
Stéphane Gely
- Architecture et Fonction des Macromolécules Biologiques, UMR6098, CNRS, Université de Provence et Université de la Méditerranée, case 932, 163 Avenue de Luminy, 13288 Marseille Cedex 9, France
Jean-Marie Bourhis
- Architecture et Fonction des Macromolécules Biologiques, UMR6098, CNRS, Université de Provence et Université de la Méditerranée, case 932, 163 Avenue de Luminy, 13288 Marseille Cedex 9, France
- Present address: Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS Université, de Lyon, 7, passage du Vercors, 69 367 Lyon Cedex 7, France.
Xavier Morelli
- Interactions et Modulateurs de Réponses, FRE3083, CNRS, Université de Provence, 31 chemin Joseph Aiguier, 13402 Marseille Cedex 20, France
Sonia Longhi
- Architecture et Fonction des Macromolécules Biologiques, UMR6098, CNRS, Université de Provence et Université de la Méditerranée, case 932, 163 Avenue de Luminy, 13288 Marseille Cedex 9, France
- Corresponding authors. Address: AFMB-UMR 6098, CNRS et Universités d’Aix-Marseille I and II, 163 avenue de Luminy, Case 932, 13288 Marseille Cedex 09. Fax: +33(0)491266720.
Hervé Darbon
- Architecture et Fonction des Macromolécules Biologiques, UMR6098, CNRS, Université de Provence et Université de la Méditerranée, case 932, 163 Avenue de Luminy, 13288 Marseille Cedex 9, France

Received 29 October 2008; received in revised form 19 February 2009; accepted 2 March 2009. published online 09 March 2009.

Abstract

In this paper we investigate the interaction between the C-terminal domains of the measles virus phosphoprotein (XD) and nucleoprotein (N_TAIL) by using nuclear magnetic resonance chemical shift perturbation experiments. Using both N_TAIL constructs and peptides, we show that contrary to the conserved Box2 region (N^489–506), the C-terminal region of N_TAIL (N^513–525) does not directly interact with XD, and yet affects binding to XD. We tentatively propose a model where the C-terminus of N_TAIL would stabilize the N_TAIL–XD complex either via a functional coupling with N^489–506 or by reducing the entropic penalty associated to the binding-coupled-to-folding process.

Structured summary

MINT-7009780, MINT-7009793, MINT-7009808: N-tail (uniprotkb:Q89933) and P (uniprotkb:P03422) bind (MI:0407) by nuclear magnetic resonance (MI:0077)

Abbreviations: MV, Measles Virus, N, nucleoprotein, L, large protein, P, phosphoprotein, PMD, P multimerization domain, PNT, P N-terminal domain, PCT, P C-terminal domain, XD, X domain, N_TAIL, C-terminal unstructured domain of N, MoRE, MOlecular Recognition Element, NMR, nuclear magnetic resonance, HSQC, heteronuclear single quantum correlation, nOe, nuclear Overhauser effect, DMSO, dimethyl sulfoxide