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.
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.
Jonák
J
J
Institute of Molecular Genetics, Czechoslovak Academy of Sciences, Prague.
Karas
K
K
D000590:Amino Acid Chloromethyl Ketones / Q000494:pharmacology*; D001412:Bacillus subtilis / Q000032:analysis*; D004926:Escherichia coli / Q000032:analysis; D001411:Geobacillus stearothermophilus / Q000032:analysis; D010444:Peptide Elongation Factor Tu / Q000378:metabolism*; D012345:RNA, Transfer, Amino Acid-Specific / Q000378:metabolism*; D012360:RNA, Transfer, Phe / Q000378:metabolism*; D014108:Tosylphenylalanyl Chloromethyl Ketone / Q000494:pharmacology*
D000590:Amino Acid Chloromethyl Ketones; D012345:RNA, Transfer, Amino Acid-Specific; D012360:RNA, Transfer, Phe; D014108:Tosylphenylalanyl Chloromethyl Ketone; D010444:Peptide Elongation Factor Tu