PMID:16825247
| Citation |
Tomoo, K, Abiko, F, Miyagawa, H, Kitamura, K and Ishida, T (2006) Effect of N-terminal region of eIF4E and Ser65-phosphorylation of 4E-BP1 on interaction between eIF4E and 4E-BP1 fragment peptide. J. Biochem. 140:237-46 |
|---|---|
| Abstract |
To clarify the contribution of N-terminal region of eukaryotic initiation factor 4E (eIF4E) to the interaction with 4E-BP and to investigate the effect of 4E-BP phosphorylation on the interaction with eIF4E, the interaction profiles of the Ser65-unphosphorylated and phosphorylated peptides (Thr37-Thr70 fragment of 4E-BP1) with full-length and N-terminal 33 residues-deleted eIF4Es were investigated by fluorescence and SPR methods. The effect of N-terminal region of eIF4E on the interaction with 4E-BP1 peptides was shown to be dependent on the interaction state, that is, the steady-state fluorescence and kinetic-state SRP analyses showed the positive and negative contributions of the N-terminal region to the interaction with the peptide, respectively, despite its unphosphorylated or phosphorylated state. The comparison of the association constants of the peptide with those of full-length 4E-BP1 indicated the importance of N-terminal (1-36) and/or C-terminal (71-118) sequence of 4E-BP1 for the interaction, although the MD simulations suggested that the alpha-helical region (Arg56-Cys62) of 4E-BP1 peptide is sufficient for keeping the interaction. The MD simulations also indicated that a charge-dependent rigid hydration shell formed around the phosphate group makes the molecular conformation rigid, and single Ser65 phosphorylation is insufficient for releasing 4E-PB1 peptide from eIF4E. |
| Links |
PubMed Online version:10.1093/jb/mvj143 |
| Keywords |
Adaptor Proteins, Signal Transducing/chemistry; Adaptor Proteins, Signal Transducing/metabolism; Amino Acid Sequence; Binding Sites; Eukaryotic Initiation Factor-4E/chemistry; Eukaryotic Initiation Factor-4E/metabolism; Models, Molecular; Molecular Sequence Data; Phosphoproteins/chemistry; Phosphoproteins/metabolism; Phosphorylation; Protein Binding; Protein Conformation |
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