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Updated: Aug 30, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
Published on: May 1, 2020
Influence of the length of the phosphate chain in mRNA 5' cap analogues on their interaction with eukaryotic
Joanna Zuberek1, Jacek Jemielity, Anna Niedzwiecka
1Department of Biophysics, Institute of Experimental Physics, Warsaw University, Warszawa, Poland.
Abstract:
The recognition of the 5'mRNA cap structure m7G(5')ppp(5')N by one of the components of the initiation translation machinery, the eIF4E factor, plays a pivotal role in regulation of the protein synthesis. In the present study we have shown two opposing roles of the cap phosphate chain in the specific eIF4E-cap interaction. The extension of the phosphate chain enhances the binding of the cap to the unphosphorylated eIF4E but destabilises the eIF4E-cap complex in case of the phosphorylated protein.
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