RNA-mediated sequestration of the RNA helicase eIF4A by Pateamine A inhibits translation initiation |
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Authors: | Bordeleau Marie-Eve Cencic Regina Lindqvist Lisa Oberer Monika Northcote Peter Wagner Gerhard Pelletier Jerry |
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Institution: | Department of Biochemistry, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montreal, Quebec H3G 1Y6, Canada. |
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Abstract: | Eukaryotic initiation factor 4A (eIF4A) is a member of the DEAD-box family of putative RNA helicases whose members are involved in many aspects of RNA metabolism. eIF4A is thought to facilitate binding of 43S preinitiation complexes to mRNAs by unwinding secondary structures present in the 5' untranslated region. Pateamine A, a small-molecule inhibitor of translation initiation, acts in an unusual manner by stimulating eIF4A activity. Herein, we report the elucidation of pateamine's mode of action. We demonstrate that Pateamine A is a chemical inducer of dimerization that forces an engagement between eIF4A and RNA and prevents eIF4A from participating in the ribosome-recruitment step of translation initiation. |
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Keywords: | CHEMBIOL RNA |
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