Influence of the length of the phosphate chain in mRNA 5' cap analogues on their interaction with eukaryotic initiation factor 4E.

Joanna Zuberek, Jacek Jemielity, Anna Niedzwiecka, Janusz Stepinski, Aleksandra Wyslouch-Cieszynska, Ryszard Stolarski, Edward Darzynkiewicz

Journal: Nucleosides, nucleotides & nucleic acids 2003;22(5-8):1707-10

PMID: 14565501

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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.

Address: Department of Biophysics, Institute of Experimental Physics, Warsaw University, Warszawa, Poland.

DOI: 10.1081/NCN-120023119

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MeSH Terms: Eukaryotic Initiation Factor-4E, Kinetics, Peptide Chain Initiation, Translational, Phosphates, Protein Binding, RNA Caps, Structure-Activity Relationship, Substrate Specificity