AI Article Synopsis
- The initiation of mRNA 5' cap-dependent translation is a key control point in eukaryotic cells that regulates protein synthesis.
- Research findings show that the human translation inhibitor, eIF4E-binding protein (4E-BP1), has a stronger affinity for the translation factor eIF4E when it is bound to the 5' cap of mRNA.
- The binding of 4E-BP1 not only stabilizes the active form of eIF4E but also promotes the release of eIF4E from the mRNA cap, highlighting a complex regulatory mechanism for controlling translation initiation.
Article Abstract
Initiation is the rate-limiting step during mRNA 5' cap-dependent translation, and thus a target of a strict control in the eukaryotic cell. It is shown here by analytical ultracentrifugation and fluorescence spectroscopy that the affinity of the human translation inhibitor, eIF4E-binding protein (4E-BP1), to the translation initiation factor 4E is significantly higher when eIF4E is bound to the cap. The 4E-BP1 binding stabilizes the active eIF4E conformation and, on the other hand, can facilitate dissociation of eIF4E from the cap. These findings reveal the particular allosteric effects forming a thermodynamic cycle for the cooperative regulation of the translation initiation inhibition.
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| http://dx.doi.org/10.1016/j.febslet.2013.10.043 | DOI Listing |
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