Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR.
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.
Bernard
Cedric
C
Architecture et Fonction des Macromolécules Biologiques, UMR6098, CNRS, Université de Provence et Université de la Méditerranée, Marseille Cedex 9, France. Cedric.Bernard@afmb.univ-mrs.fr
Gely
Stéphane
S
Bourhis
Jean-Marie
JM
Morelli
Xavier
X
Longhi
Sonia
S
Darbon
Hervé
H
D008459:Measles virus / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D019590:Nucleocapsid Proteins / Q000737:chemistry* / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000502:physiology; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism
D019590:Nucleocapsid Proteins; C055859:P protein, Sendai virus; D010750:Phosphoproteins; D014764:Viral Proteins