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...

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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
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author Gosselin, Pauline
Oulhen, Nathalie
Jam, Murielle
Ronzca, Justyna
Cormier, Patrick
Czjzek, Mirjam
Cosson, Bertrand
author_facet Gosselin, Pauline
Oulhen, Nathalie
Jam, Murielle
Ronzca, Justyna
Cormier, Patrick
Czjzek, Mirjam
Cosson, Bertrand
author_sort Gosselin, Pauline
collection PubMed
description 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.
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spelling pubmed-30828852011-04-27 The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS Gosselin, Pauline Oulhen, Nathalie Jam, Murielle Ronzca, Justyna Cormier, Patrick Czjzek, Mirjam Cosson, Bertrand Nucleic Acids Res Structural Biology 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. Oxford University Press 2011-04 2010-12-22 /pmc/articles/PMC3082885/ /pubmed/21183464 http://dx.doi.org/10.1093/nar/gkq1306 Text en © The Author(s) 2010. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/2.5 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Structural Biology
Gosselin, Pauline
Oulhen, Nathalie
Jam, Murielle
Ronzca, Justyna
Cormier, Patrick
Czjzek, Mirjam
Cosson, Bertrand
The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS
title The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS
title_full The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS
title_fullStr The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS
title_full_unstemmed The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS
title_short The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS
title_sort translational repressor 4e-bp called to order by eif4e: new structural insights by saxs
topic Structural Biology
url 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
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