| Title: |
Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral-mediated proteases |
| Authors: |
Martin Bushell; Wendy Wood; Gillian Carpenter; Virginia M Pain; Simon Morley; Michael J Clemens |
| Publication Year: |
2001 |
| Collection: |
University of Sussex (US): Figshare |
| Subject Terms: |
Uncategorised value |
| Description: |
Eukaryotic initiation factor (eIF) 4B interacts with several components of the initiation pathway and is targeted for cleavage during apoptosis. In a cell-free system, cleavage of eIF4B by caspase-3 coincides with a general inhibition of protein synthetic activity. Affinity chromatography demonstrates that mammalian eIF4B interacts with the poly(A)-binding protein and that a region consisting of the N-terminal 80 amino acids of eIF4B is both necessary and sufficient for such binding. This interaction is lost when eIF4B is cleaved by caspase-3, which removes the N-terminal 45 amino acids. Similarly, the association of eIF4B with the poly(A)-binding proteinin vivo is reduced when cells are induced to undergo apoptosis. Cleavage of the poly(A)-binding protein itself, using human rhinovirus 3C protease, also eliminates the interaction with eIF4B. Thus, disruption of the association between mammalian eIF4B and the poly(A)-binding protein can occur during both apoptosis and picornaviral infection and is likely to contribute to the inhibition of translation observed under these conditions. |
| Document Type: |
article in journal/newspaper |
| Language: |
unknown |
| Relation: |
10779/uos.23330375.v1 |
| Availability: |
https://figshare.com/articles/journal_contribution/Disruption_of_the_interaction_of_mammalian_protein_synthesis_eukaryotic_initiation_factor_4B_with_the_poly_A_-binding_protein_by_caspase-_and_viral-mediated_proteases/23330375 |
| Rights: |
Copyright not evaluated |
| Accession Number: |
edsbas.9EDC946E |
| Database: |
BASE |