Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR |
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Authors: | Cedric Bernard,Sté phane Gely,Xavier Morelli,Hervé Darbon |
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Affiliation: | a 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 b Interactions et Modulateurs de Réponses, FRE3083, CNRS, Université de Provence, 31 chemin Joseph Aiguier, 13402 Marseille Cedex 20, France |
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Abstract: | In this paper we investigate the interaction between the C-terminal domains of the measles virus phosphoprotein (XD) and nucleoprotein (NTAIL) by using nuclear magnetic resonance chemical shift perturbation experiments. Using both NTAIL constructs and peptides, we show that contrary to the conserved Box2 region (N489-506), the C-terminal region of NTAIL (N513-525) does not directly interact with XD, and yet affects binding to XD. We tentatively propose a model where the C-terminus of NTAIL would stabilize the NTAIL-XD complex either via a functional coupling with N489-506 or by reducing the entropic penalty associated to the binding-coupled-to-folding process.Structured summaryMINT-7009780, MINT-7009793, MINT-7009808: N-tail (uniprotkb:Q89933) and P (uniprotkb:P03422) bind (MI:0407) by nuclear magnetic resonance (MI:0077) |
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Keywords: | 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 NTAIL, 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 |
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