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- W22772503 abstract "As is true for bacterial systems, GTP is the nucleotide which drives eukaryotic protein synthesis (Merrick 1992). The primary use of ATP is in the activation of amino acids to provide aminoacyl-tRNAs, the chemically activated form of the amino acid. There are three discrete steps in eukaryotic protein synthesis: initiation, elongation, and termination. As indicated in Table 1, each of these steps is associated with specific factors which bind and hydrolyze GTP. The eukaryotic initiation factor 2 (eIF-2) is the central factor in initiation and binds GTP and the initiator tRNA, Met-tRNAi. The ternary complex of eIF-2, GTP, and Met-tRNAi is bound to the 40S subunit and serves to locate the initiating AUG. Upon recognition of the AUG codon, the ternary complex is then susceptible to the action of eIF-5, which triggers the hydrolysis of GTP and leads to the release of eIF-2 · GDP from the ribosome. A curious feature of eIF-5 is that it also possesses a ribosome-dependent GTPase activity which is required in model assays using eIF-2A in place of eIF-2 to form initiation complexes (Adams et al. 1975; Merrick et al. 1975).KeywordsElongation FactorTranslation FactorEukaryotic Initiation FactorEuglena GracilisMycoplasma HominisThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves." @default.
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- W22772503 date "1993-01-01" @default.
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- W22772503 title "Eukaryotic Translation Factors Which Bind and Hydrolyze GTP" @default.
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