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Extra info for Progress in Nucleic Acid Research and Molecular Biology, Vol. 22

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ATP, after periodate oxidation and borohydride reduction (ATP,xi-red)is not a substrate for the yeast transferase (142). Finally, modification of the phosphate groups of ATP by replacement of the a-0x0 group of the triphosphate side-chain by a sulfur atom has been investigated. Adenosine 5’-(a,y)dithiotriphosphateand adenosine 5’-(y-thio)triphosphateare not substrates for the yeast enzyme (112). Analogs of cytidine can be incorporated into tRNA-N or tRNA-N-C. In all cases investigated, no difference was observed in the ability of analogs to replace cytidylic acid in one of the two penultimate positions.

I 4 5 W 5 2 h 38 MATHIAS SPRINZL AND FRIEDRICH CRAMER could be predicted from experiments with deoxy tRNAs, tRNAPhe-AC-C-A(3’NH2) is aminoacylated whereas tRNAPhe-A-C-C-A(2‘NH2)is not (Table V). Although the determination of the site of aminoacylation using “amino” tRNAs (125, 138) is more complicated than that using the isomeric “deoxy” species for the above mentioned reasons, the nonisomerizable products of aminoacylation of tRNA-N-C-C-A(2‘NH2) or tRNA-N-C-C-A(3‘NH2)(Fig. 7d,e) are very usefuI for the study of 2‘ vs.

THE -C-C-A END OF tRNA 13 tRNAPhe. If a conformational difference between Phe-tRNAphe and tRNAPheexists, it is not understood how it may be maintained when the tRNA is free in solution. It is possible that the thermodynamic barrier between the two conformations is so small that the particular native form of Phe-tRNAPheis not preserved during the preparation and isolation procedure. It is likely that the changes upon aminoacylation observed b y X-ray laser-light scattering (95),sedimentation behavior (101, scattering (82), 102),and an NMR study of manganese binding sites (83) are due to perturbations in the shell of counterions.

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