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Contenuto archiviato il 2024-05-29

Characterization of the structure and dynamics of a protein complex indispensable for RNA synthesis in Sendai Virus

Obiettivo

Sendai Virus (SeV) is a prototype of viruses with a negative strand RNA genome. This family of viruses causes important human and animal diseases. RNA synthesis in these viruses requires the placement of the RNA polymerase on the nucleocapsid that assemble s the RNA. This occurs through an interaction between two protein domains: the partly folded PX domain of phosphoprotein P that is part of the polymerase, and the unstructured N-tail domain of nucleocapsid protein N.

For transcribing the template RNA, the polymerase needs to move along the RNA, which requires PX to on and off interact with N-tail domains on subsequent nucleocapsids. This suggests that flexibility is a key issue in the biological function of these domains. This project will study the structure and dynamics of this protein complex by NMR, in order to arrive at a better understanding of the transcription process in this family of viruses. Both PX (partly) and N-tail belong to the class of intrinsically unstructured proteins (IUPs), which encompasses around 25% of all eukaryotic proteins. NMR is one of the sole techniques that are capable of studying this class proteins and this project aims at improving NMR methodology optimised for IUPs.

The project is part of an ongoing collaboration between the host lab and virus group of Prof. R. Ruigrok at the EMBL in Grenoble. This allows me to both acquire skills related to molecular biology as well as to enlarge my knowledge of NMR in order to further develop myself as a bio-molecular NMR spectroscopist. Furthermore, the experiences in NMR application and methodology acquired during my PhD will prove very valuable for the realization of the project.

Campo scientifico (EuroSciVoc)

Parole chiave

Argomento(i)

Invito a presentare proposte

FP6-2002-MOBILITY-5
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Meccanismo di finanziamento

EIF - Marie Curie actions-Intra-European Fellowships

Coordinatore

INSTITUT DE BIOLOGIE STRUCTURALE JEAN-PIERRE EBEL
Contributo UE
Nessun dato
Indirizzo


Francia
Costo totale
Nessun dato