Modification of Bacillus subtilis elongation factor Tu by N‐tosyl‐L phenylalanyl chloromethane abolishes its ability to interact with the 3′‐terminal polynucleotide structure but not with the acyl bond in aminoacyl‐tRNA

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Abstract
Modification of B. subtilis EF-TU by N-tosyl-L-phenylalanyl chloromethane destroyed its ability to promote protein synthesis and resulted in selective dissociation of the two binding activities of the protein for aminoacyl-tRNA. The modified EF-Tu was completely ineffective in the protection of the 3′-terminal CCA structure of tRNA against pancreatic ribonuclease, while remaining almost fully active in the protection of the ester bond between the 3′-terminal adenosine and the amino acid residue in aminoacyl-tRNA.

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