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Deaggregation of eIF4E induced by mRNA 5' cap binding.

Anna Niedzwiecka·Edward Darzynkiewicz·Ryszard Stolarski
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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 m7G7P, progressive deaggregation with the time of incubation in the presence of the cap analogue has been observed.

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AnimalsEscherichia coliEukaryotic Initiation Factor-4EKineticsLightMacromolecular SubstancesMiceModels, ChemicalPeptide Initiation FactorsPhosphatesProtein BindingProtein ConformationProtein Structure, TertiaryProtonsRNA Cap AnalogsRNA CapsRNA, MessengerScattering, RadiationTime FactorsJournal ArticleResearch Support, Non-U.S. Gov't

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Anna Niedzwiecka, Edward Darzynkiewicz, Ryszard Stolarski. 2005. Deaggregation of eIF4E induced by mRNA 5' cap binding.. https://doi.org/10.1081/ncn-200061784

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