Specific functional interactions of nucleotides at key (super -)3 and (super +)4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex

Article Abstract:

Eukaryotic initiation factor (eIF) 1 maintains the fidelity of initiation codon selection and enables mammalian 48S preinitiation complexes to discriminate against AUG codons, in which the purines at (super -)3 and (super +)4 positions are most important. Results of UV cross-linking experiments and assays of 48S complex formation done indicate that eIF2alpha's interaction with the (super -)3 purine is responsible for recognition of the (super -)3 context position by 48S complexes.

United States, Biological Product (except Diagnostic) Manufacturing, Nucleic Acid Derivatives, Nucleotides, Genetic translation, Translation (Genetics), Genetic code

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Position of eukaryotic initiation factor eIFI on the 40S ribosomal subunit determined by directed hydroxyl radical probing

Article Abstract:

The position of eukaryoic initiation factor (e1F1) on the 40S ribosomal subunit is determined using directed hydroxyl radical cleavage to understand the discriminatory role played by e1F1. The position of eIF1 on the 40S subunit suggests that its position close to the P-site is very favorable for an indirect mechanism of eIF1's action.

Cells (Biology), Cells, Hydroxylases, Genetic research

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Structural basis for the enhancement of eIF4A helicase activity by eIF4G

Article Abstract:

The eukaryotic translation initiation factors 4A (eIF4A) and 4G (eIF4G) are crucial for the assembly of the translationally active ribosome. Even though both eIF4A domains play a role in binding the middle domain of eIF4G, the main interaction surface is located on the C-terminal domain.

Drugs, Cellular Protein, In-Vitro Diagnostic Substance Manufacturing, Eukaryotes, Cellular proteins

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