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J. Biol. Chem., Vol. 278, Issue 20, 18638-18648, May 16, 2003
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From the The nucleoprotein of measles virus
consists of an N-terminal moiety, NCORE, resistant to
proteolysis and a C-terminal moiety, NTAIL, hypersensitive
to proteolysis and not visible as a distinct domain by electron
microscopy. We report the bacterial expression, purification, and
characterization of measles virus NTAIL. Using nuclear
magnetic resonance, circular dichroism, gel filtration, dynamic light
scattering, and small angle x-ray scattering, we show that
NTAIL is not structured in solution. Its sequence and spectroscopic and hydrodynamic properties indicate that
NTAIL belongs to the premolten globule subfamily within the
class of intrinsically disordered proteins. The same epitopes are
exposed in NTAIL and within the nucleoprotein, which rules
out dramatic conformational changes in the isolated NTAIL
domain compared with the full-length nucleoprotein. Most unstructured
proteins undergo some degree of folding upon binding to their partners,
a process termed "induced folding." We show that NTAIL
is able to bind its physiological partner, the phosphoprotein, and that
it undergoes such an unstructured-to-structured transition upon binding
to the C-terminal moiety of the phosphoprotein. The presence of
flexible regions at the surface of the viral nucleocapsid would enable plastic interactions with several partners, whereas the gain of structure arising from induced folding would lead to modulation of
these interactions. These results contribute to the study of the
emerging field of natively unfolded proteins.
The C-terminal Domain of the Measles Virus Nucleoprotein Is
Intrinsically Disordered and Folds upon Binding to the C-terminal
Moiety of the Phosphoprotein*
§,,¶,
,,, and
Architecture et Fonction des
Macromolécules Biologiques, UMR 6098 CNRS et Université
Aix-Marseille I et II, ESIL, Campus de Luminy, 13288 Marseille Cedex
09, France, ** MRC Virology Unit, Institute of Virology,
Church St., Glasgow G11 5JR, United Kingdom, and
European Synchrotron Radiation Facility, BP
220, 38043 Grenoble Cedex, France
*
This work was supported in part by the CNRS. This study has
been carried out with financial support from the Commission of the
European Communities, specific program "Quality of Life and Management of Living Resources," QLK2-CT2001-01225, "Towards the Design of New Potent Antiviral Drugs: Structure-Function Analysis of
Paramyxoviridae RNA Polymerase."The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by a postdoctoral fellowship from the EMBO.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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