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- W2300926400 abstract "[Eukaryotic protein synthesis requires two protein factors which bind aminoacyl-tRNA in a GTP-dependent manner. One, initiation factor 2 (eIF-2), binds only the initiator Met-tRNA{dollar}{bsol}sb{lcub}{bsol}rm i{rcub}{dollar} and carries it to the 40S subunit of the ribosome. The other, elongation factor 1a (EF-1a) binds all other aminoacyl-tRNAs to the elongating 80S ribosome. The goal of this thesis is to characterize the structural aspects of these proteins. EF-1a is similar to the amino acid level to Escherichia coli EF-Tu, a protein for which the X-ray crystal structure is known. The limited trypsin cleavage used for the EF-Tu crystal structure was performed on EF-1a. The catalytic activity as measured by several assays is reduced, the binding of the ribosome and aminoacyl-tRNA is partially maintained and GRP binding is near wild type. The aminoacyl-tRNA binding site has been localized on EF-1a by chemical crosslinking using three tRNA species and two crosslinking reagents, trans-diaminedicholoro platium (II) and diepoxybutane. The aminoacyl binding region has been determined by crosslinking of N{dollar}{bsol}sp{lcub}{bsol}epsilon{rcub}{dollar}-bromoacetyl-Lys-tRNA. A model for the structure of EF-1a is proposed. When the crosslinking results are compared to this model, all the reactive residues appear to be on one face of the molecule. Studies of aminoacyl-tRNA protection of EF-1a from protease digestion support these results. The initiation factor eIF-2 is less well characterized than the elongation factor. The protein contains three subunits. The {dollar}{bsol}beta{dollar} and {dollar}{bsol}gamma{dollar} subunits and two proteins which have been proposed to interact with eIF-2 have been partially sequenced at the amino acid level. To determine the function of the subunits of eIF-2, subunit deficient forms were used in the three in vitro assays. The results implicate a role for the {dollar}{bsol}beta{dollar} subunit in both Met-tRNA{dollar}{bsol}sb {lcub}{bsol}rm i{rcub}{dollar} and GTP binding, and the possibility of a shared GTP site between the {dollar}{bsol}beta{dollar} and {dollar}{bsol}gamma{dollar} subunits. GTP crosslinking and affinity labeling indicate only the {dollar}{bsol}beta{dollar} subunit in GTP binding. Met-tRNA{dollar}{bsol}sb{lcub}{bsol}rm i{rcub}{dollar} crosslinking indicates the {dollar}{bsol}beta{dollar} ands {dollar}{bsol}gamma{dollar} subunits both participate in binding.]" @default.
- W2300926400 created "2016-06-24" @default.
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- W2300926400 date "1991-01-01" @default.
- W2300926400 modified "2023-09-26" @default.
- W2300926400 title "Characterization of GTP and aminoacyl-tRNA binding to eukaryotic initiation factor 2 and elongation factor 1" @default.
- W2300926400 hasPublicationYear "1991" @default.
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