The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS

eIF4E binding protein (4E-BP) inhibits translation of capped mRNA by binding to the initiation factor eIF4E and is known to be mostly or completely unstructured in both free and bound states. Using small angle X-ray scattering (SAXS), we report here the analysis of 4E-BP structure in solution, which...

Descripción completa

Detalles Bibliográficos
Autores principales: Gosselin, Pauline, Oulhen, Nathalie, Jam, Murielle, Ronzca, Justyna, Cormier, Patrick, Czjzek, Mirjam, Cosson, Bertrand
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2011
Materias:
Structural Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3082885/
https://www.ncbi.nlm.nih.gov/pubmed/21183464
http://dx.doi.org/10.1093/nar/gkq1306
Descripción
Sumario:eIF4E binding protein (4E-BP) inhibits translation of capped mRNA by binding to the initiation factor eIF4E and is known to be mostly or completely unstructured in both free and bound states. Using small angle X-ray scattering (SAXS), we report here the analysis of 4E-BP structure in solution, which reveals that while 4E-BP is intrinsically disordered in the free state, it undergoes a dramatic compaction in the bound state. Our results demonstrate that 4E-BP and eIF4E form a ‘fuzzy complex’, challenging current visions of eIF4E/4E-BP complex regulation.

Ejemplares similares