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Interaction between yeast eukaryotic initiation factor eIF4E and mRNA 5' cap analogues differs from that for murine eIF4E.

Katarzyna Kiraga-Motoszko·Janusz Stepinski·Anna Niedzwiecka·Jacek Jemielity·Malgorzata Wszelaka-Rylik·Ryszard Stolarski·Wojciech Zielenkiewicz·Edward Darzynkiewicz
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Abstract

Measurements of interaction of 7-methyl-GTP eIF4E from S. cerevisiae were performed by means of two methods: Isothermal Titration Calorimetry (ITC) and fluorescence titration. The equilibrium association constants (Kas) derived from the two methods show significantly different affinity of yeast eIF4E for the mRNA 5' cap than those of the murine and human proteins. The observed differences in the Kas values and the enthalpy changes of the association (deltaH(o)) suggest some dissimilarity in the mode of binding and stabilization of cap in the complexes with eIF4E from various sources.

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AnimalsBinding SitesCalorimetryEukaryotic Initiation Factor-4EMiceRNA Cap AnalogsRNA CapsRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpecies SpecificitySpectrometry, FluorescenceThermodynamicsComparative StudyJournal ArticleResearch Support, Non-U.S. Gov't

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Katarzyna Kiraga-Motoszko, Janusz Stepinski, Anna Niedzwiecka, Jacek Jemielity, Malgorzata Wszelaka-Rylik, Ryszard Stolarski, Wojciech Zielenkiewicz, Edward Darzynkiewicz. Interaction between yeast eukaryotic initiation factor eIF4E and mRNA 5' cap analogues differs from that for murine eIF4E.. https://doi.org/10.1081/ncn-120023120

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