Abstract
WE have isolated a strain of Escherichia coli K-12 bacteria that we believe to be conditionally defective in peptidyl-tRNA hydrolase. This enzyme (which we shall refer to as hydrolase) catalyses the hydrolysis of peptidyl-tRNA (or N-acyl-amino-acyl-tRNA) yielding free peptide (or N-acyl-amino-acid) and a tRNA capable of accepting its conjugate amino-acid1,2. In the current model of protein biosynthesis3 peptidyl-tRNA is the form in which the growing protein is bound to the ribosome. Ribosome-bound peptidyl-tRNA, however, is a poor substrate for the hydrolase2,4, implying that the normal substrate is free. N-acyl-aminoacyl-tRNAs occur in cells5–7 but the only species the function of which is known3,8, N-formyl-methionyl-tRNAf, is a poor substrate for bacterial peptidyl-tRNA hydrolase1,9,10.
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ATHERLY, A., MENNINGER, J. Mutant E. coli Strain with Temperature Sensitive Peptidyltransfer RNA Hydrolase. Nature New Biology 240, 245–246 (1972). https://doi.org/10.1038/newbio240245a0
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DOI: https://doi.org/10.1038/newbio240245a0
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