Circular dichroism and fluorescence studies on protein synthesis initiation factor eIF-4E and two mutant forms from the yeast Saccharomyces cerevisiae.
作者： W D McCubbin , I Edery , M Altmann , N Sonenberg , C M Kay
DOI: 10.1016/S0021-9258(19)77888-0
关键词:
摘要: Abstract Circular dichroism studies have shown that eukaryotic initiation factor 4E contains low amounts of alpha-helix; the main elements secondary structure are beta-sheets/turns and aperiodic regions. Interactions with cap analogs accompanied by small but reproducible changes in overall structure, which may also involve more significant perturbations localized regions containing certain phenylalanine residues. Dissociation constants for interactions nucleotides been established from fluorescence titrations. Results show (N-7) methylated guanosine bound strongly than their nonmethylated counterparts. Involvement a key tryptophan residue binding site was suggested. Additional two mutant forms protein, designated SK-4 (W----75----L) SK-6 (W----115----L), confirmed extended these observations. Fluorescence melting experiments indicated stabilized protein against thermal perturbation demonstrated subtle differences folding between wild-type protein. These account observed loss specificity both forms.
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