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• W2016795884 abstract "The possible role of guanosine 5′-triphosphate,3′-diphosphate (pppGpp) in protein synthesis by Escherichia coli ribosomes and protein factors was examined. Although pppGpp could effectively substitute for GTP in reactions catalyzed by initiation factor 2 (ribosomal binding of fMet-tRNA and formation of N -formylmethionylpuromycin) and elongation factor T (ribosomal binding of Phe-tRNA and formation of dipeptidyl-tRNA), pppGpp poorly supported polyphenylalanine synthesis. The interaction of elongation factor G with pppGpp was, therefore, examined in detail. The nucleotide was found to be almost without activity in the translocation reaction, as measured by formation of N -acetylphenylalanyl-phenylalanylpuromycin. Nevertheless, the rate of the catalytic hydrolysis of pppGpp to guanosine 5′-diphosphate,3′-diphosphate by elongation factor G and ribosomes was about 30% of the rate of hydrolysis of GTP, a rate of hydrolysis that significantly exceeded the rate of translocation with GTP. Moreover, the rates of the fusidic acid-dependent, elongation factor G-dependent binding of pppGpp and ppGpp to ribosomes were about 75 to 85% the rates of GTP and GDP binding, respectively. We also found that dGTP could substitute for GTP in all reactions examined." @default.
• W2016795884 created "2016-06-24" @default.
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• W2016795884 date "1973-11-01" @default.
• W2016795884 modified "2023-10-17" @default.
• W2016795884 title "Role of Guanine Nucleotides in Protein Synthesis. Elongation Factor G and Guanosine 5′-Triphosphate,3′-Diphosphate" @default.
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• W2016795884 doi "https://doi.org/10.1073/pnas.70.11.3250" @default.
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