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PubMed · 2016328

Evidence that eukaryotic initiation factor (eIF) 2 is a cap-binding protein that stimulates cap recognition by eIF-4B and eIF-4F.

H A van Heugten·M A Kasperaitis·A A Thomas·H O Voorma
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Abstract

We studied the mRNA-binding properties of eukaryotic initiation factor (eIF) 2. This Met-tRNA-binding factor interacts with the cap structure of reoviral mRNA in an ATP-independent manner. Both the beta- and gamma-subunit of eIF-2 are involved in the UV-induced cross-linking of eIF-2 to the cap. The interaction of eIF-2 with a messenger is sensitive to the cap analogue 7-methyl-guanosine 5'-triphosphate as measured by cross-linking and by mRNA retention on nitrocellulose filters. The cap-binding property of eIF-2 does not conflict with the current mRNA-binding model of initiation factors eIF-4A, -4B, and -4F: cross-linking of eIF-4E and of eIF-4B is stimulated by eIF-2. The eIF-2-mediated increase of eIF-4E interaction results in a decrease of the cross-linking of the beta- and gamma-subunits of eIF-2. The presence of GTP in the cross-linking assay interferes with the interaction of eIF-2 with the cap structure but does not inhibit the eIF-2 stimulated eIF-4E and -4B cross-linking. These observations indicate a role for eIF-2 in the mRNA recognition.

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AnimalsCell LineEukaryotic Initiation Factor-2Eukaryotic Initiation Factor-4FEukaryotic Initiation FactorsKineticsMammalian orthoreovirus 3Peptide Initiation FactorsProtein BindingRNA CapsRNA, MessengerUltraviolet RaysJournal Article

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H A van Heugten, M A Kasperaitis, A A Thomas, H O Voorma. 1991-04-15. Evidence that eukaryotic initiation factor (eIF) 2 is a cap-binding protein that stimulates cap recognition by eIF-4B and eIF-4F.. https://pubmed.ncbi.nlm.nih.gov/2016328/

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