Abstract
AMINO acid starvation of rel+ bacteria1 results in a rapid pleiotropic response involving the cessation of stable RNA synthesis, a decrease in the rate of nucleoside transport, an altered pattern of mRNA synthesis, inhibition of phospholipid synthesis and increased protein turnover. This stringent response2 is rapidly reversed when the amino acid starvation is relieved and is apparently mediated by two unusual nucleotides, guanosine 5′-diphosphate, 3′-diphosphate (ppGpp) and guanosine 5′-triphosphate, 3′-diphosphate (pppGpp)3. These nucleotides are synthesised on the ribosome in the presence of uncharged tRNA, ATP, GTP and an enzyme known as stringent factor3. Mutants which fail to exhibit the stringent response to amino acid starvation with the synthesis of ppGpp pppGpp are known as relaxed mutants4 and in Escherichia coli are mapped at three loci; relA (ref. 5), relB (ref. 6), and rplK (relC) (refs 7 and 8). The synthesis of ppGpp and pppGpp has also been observed in various prokaryotes including blue-green algae9. Here we demonstrate the ability of bacterial stringent factor to be stimulated by eukaryotic ribosomal preparations to synthesise both ppGpp and pppGpp.
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POLLARD, J., PARKER, J. Guanosine tetra- and pentaphosphate synthesis by bacterial stringent factor and eukaryotic ribosomes. Nature 267, 371–373 (1977). https://doi.org/10.1038/267371a0
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DOI: https://doi.org/10.1038/267371a0
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