Alteration of the major phosphorylation site of eukaryotic protein synthesis initiation factor 4E prevents its association with the 48 S initiation complex.

Abstract excerpt

Site-directed mutagenesis was used to replace the serine residue at the primary phosphorylation site of human eukaryotic initiation factor (eIF) 4E with an alanine residue. The mutated cDNA was transcribed in vitro, and the transcript was used to direct protein synthesis in a reticulocyte lysate system. The variant protein (eIF-4EAla) was retained on a 7-methylguanosine 5'-triphosphate (m7GTP)-Sepharose affinity...

Topics

• Alanine
• Cell-Free System
• Centrifugation, Density Gradient
• Chromatography, Affinity
• Eukaryotic Initiation Factor-4E
• Humans
• Isoelectric Focusing
• Kinetics
• Mutation
• Peptide Chain Initiation, Translational