title: The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS.
abstract: 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.
authors.affiliation: UPMC Univ Paris 06, UMR 7150, Mer et Santé, Equipe Traduction Cycle Cellulaire et Développement, Station Biologique de Roscoff, 29680 Roscoff, France. gosselin@sb-roscoff.fr
authors.forename: Pauline
authors.initials: P
authors.lastname: Gosselin
authors.forename: Nathalie
authors.initials: N
authors.lastname: Oulhen
authors.forename: Murielle
authors.initials: M
authors.lastname: Jam
authors.forename: Justyna
authors.initials: J
authors.lastname: Ronzca
authors.forename: Patrick
authors.initials: P
authors.lastname: Cormier
authors.forename: Mirjam
authors.initials: M
authors.lastname: Czjzek
authors.forename: Bertrand
authors.initials: B
authors.lastname: Cosson
mesh_terms: D039561:Eukaryotic Initiation Factor-4E / Q000737:chemistry* / Q000378:metabolism; D039642:Eukaryotic Initiation Factors / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D053838:Scattering, Small Angle; D020539:Sequence Analysis, Protein; D014961:X-Ray Diffraction
chemical_list: D039561:Eukaryotic Initiation Factor-4E; D039642:Eukaryotic Initiation Factors