Involvement of eukaryotic initiation factor 4A in the cap recognition process.
Antibodies against eukaryotic initiation factor 4A (eIF-4A) were used to study the involvement of this factor in recognizing the 5' cap structure of eukaryotic mRNA. We demonstrate that an approximately 50-kilodalton polypeptide present in rabbit reticulocyte ribosomal high salt wash which can be specifically cross-linked to the 5' oxidized cap structure of reovirus mRNA (Sonenberg, N. (1981) Nucleic Acids Res. 9, 1643) reacts with an anti-eIF-4A monoclonal antibody. We also show that antibodies against eIF-4A react with a 50-kilodalton polypeptide present in a cap-binding protein complex obtained by elution from a m7GTP-agarose affinity column. Comparative peptide analysis of eIF-4A and the 50-kilodalton component of the cap-binding protein complex indicates a very strong similarity between the two polypeptides.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification; D002846:Chromatography, Affinity; D039601:Eukaryotic Initiation Factor-4A; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D010448:Peptide Initiation Factors / Q000378:metabolism*; D039381:RNA Cap-Binding Proteins; D012315:RNA Caps / Q000378:metabolism*; D011817:Rabbits; D014357:Trypsin / Q000378:metabolism
D002352:Carrier Proteins; D010446:Peptide Fragments; D010448:Peptide Initiation Factors; D039381:RNA Cap-Binding Proteins; D012315:RNA Caps; D000255:Adenosine Triphosphate; D039601:Eukaryotic Initiation Factor-4A; D014357:Trypsin