J. Hershey, R. Monro
Jun 1, 1966
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1
Influential Citations
70
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Journal
Journal of molecular biology
Abstract
Synthesis and characterization are described of a new GTP analogue, 5′-guanylyl methylenediphosphonate. A methylene bridge is substituted for oxygen between the β and γ phosphorus atoms, thus preventing enzymic cleavage at this position. The effects of this analogue on protein biosynthesis have been studied in an in vitro system from Escherichia coli. It inhibits the homopolynucleotide-directed syntheses of polyphenylalanine, polylysine and polyproline. The inhibition takes place in a resolved system, starting with phenylalanyl sRNA, and is reversed by the addition of excess GTP. The degree of inhibition depends upon the concentration ratio of GTP and the analogue. The analogue does not affect the activity of amino acyl sRNA synthetases or pyruvate kinase. It is concluded that this analogue acts as a specific, competitive inhibitor of the GTP reaction in protein synthesis.