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Résumé
Le maintien de l'intégrité du patrimoine
génétique est essentiel à la survie des organismes
vivants. Face aux nombreuses sources de stress génotoxiques qui
induisent des dommages de l'ADN,
les cellules ont mis en place des mécanismes complexes
capables de détecter et réparer ces lésions. Parmi ces
sources, figurent les rayonnements ultraviolets (UV) contenus dans la
lumière solaire, qui modifient la structure de l'ADN et peuvent conduire
à l'introduction de mutations. Chez l'homme, la grande majorité
des dommages de l'ADN produits par les rayonnements est éliminée
par le système NER (Nucleotide Excision Repair), un
système capable d'exciser les nucléotides
lésés et de les remplacer. Une déficience de cette voie
de réparation peut mener à l'apoptose (mort programmée des
cellules), et augmente la susceptibilité de développer des
maladies graves telles que le cancer. Le système NER met en
oeuvre de nombreuses protéines impliquées dans des
mécanismes variés tels que
la détection, la signalisation, ou la
réparation de l'ADN. La protéine eucaryote KIN17,
récemment découverte dans le noyau de la cellule humaine,
semble appartenir à ce système de réparation.
Cependant, son rôle précis dans la réponse aux dommages de
l'ADN reste à ce jour inconnu. C'est pourquoi, nous avons entrepris une
caractérisation structurale et fonctionnelle de la région 51-160
de
la protéine KIN17 humaine (domaine K2) afin
d'améliorer la connaissance de ses fonctions, de ses partenaires
biologiques, et de ses modes de fonctionnement.
La première partie de ce manuscrit est consacrée
à la préparation de l'échantillon de protéine
en vue d'une analyse structurale par Résonance
Magnétique Nucléaire (RMN). Le travail a dans un premier temps
consisté à choisir et optimiser le système d'expression de
domaines structuraux d'une autre protéine : la proline
déshydrogénase PRODH.
Dans un second temps, la meilleure stratégie de
préparation de l'échantillon a été appliquée
à
la protéine KIN17 pour produire, puis
résoudre la structure tridimensionnelle du domaine K2 par RMN et
Modélisation Moléculaire. Nous avons montré que la
région 51-160 de la protéine KIN17 humaine adopte un repliement
caractéristique de la famille structurale « Winged Helix
» des protéines
de liaison aux acides nucléiques. Cependant,
l'analyse des détails structuraux du domaine K2, la comparaison
avec des protéines de fonction connue de la même classe
structurale, et des études électrophorétiques,
révèlent l'incapacité de ce domaine à lier l'ADN et
l'ARN de manière autonome.
En revanche, nous avons mis en évidence, par
une étude RMN complémentaire, l'existence d'une surface
ultra conservée impliquée dans des interactions de type
protéine-protéine intra-moléculaires entre le motif
« Winged Helix » de la région 51-160 et la
région N-terminale 1-50 de KIN17 humaine.
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