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  • Title: The elongation factor Tu.GTPase reaction: effect of 2'(3')-O-aminoacyl oligoribonucleotides.
    Author: Tezuka M, Chládek S.
    Journal: Biochim Biophys Acta; 1988 Sep 07; 950(3):463-5. PubMed ID: 2844263.
    Abstract:
    The activity of synthetic (2'(3')-O-aminoacyl trinucleotides, C-C-A-Phe, C-C-U-Phe, C-U-A-Phe, U-C-A-Phe and C-A-A-Phe, in promoting the EF-Tu.70 S ribosome-catalyzed GTP hydrolysis was investigated. It was found that the activity decreases in the order C-C-A-Phe greater than C-U-A-Phe greater than U-C-A-Phe greater than C-A-A-Phe much greater than C-C-U-Phe. Thus, the substitution in 'natural' C-C-A sequence with other nucleobases weakens binding of 2'(3')-O-aminoacyl trinucleotides to EF-Tu, with the substitution at the 3'-position having the most profound effect. Since the 2'(3')-O-aminoacyl oligonucleotides mimic the effect of the aa-tRNA 3'-terminus on EF-Tu.GTPase, it follows that EF-Tu probably directly recognizes structure of nucleobases in the aa-tRNA 3'-terminus, with the 3'-terminal adenine playing the most important role.
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