DEAGGREGATION OF eIF4E INDUCED BY mRNA 5′ CAP BINDING

Abstract

All eukaryotic mRNAs contain a 5′ terminal cap structure, which consists of 7-methylguanosine linked by a 5′-5′ triphosphate bridge to the first transcribed nucleoside (m⁷GpppN). Specific recognition of the cap by the eukaryotic initiation factor eIF4E plays a key role in regulation of translation initiation as a rate-limiting step. Using dynamic light scattering (DLS), the apo-form of murine eIF4E (33–217) was shown to aggregate. After addition of m⁷GTP, progressive deaggregation with the time of incubation in the presence of the cap analogue has been observed.

Keywords:

• eIF4E
• Cap-binding
• Deaggregation
• DLS