Regulation of ornithine decarboxylase activity by guanine nucleotides: in vivo test in potassium-depleted Escherichia coli.

The observation that guanosine 5'-triphosphate (GTP) is an activator and guanosine 5'-diphosphate-3'-diphosphate (ppGpp) is an inhibitor of ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) of Escherichia coli [E. Hölttä et al. (1974) Biochem. Biophys. Res. Commun. 59, 1104-1111] has been confirmed. The hypothesis that synthesis of both polyamine and RNA in E. coli is regulated in vivo by these nucleotides was tested in E. coli B-207. On transfer of this K+-requiring, amino-acid-deficient strigent strain from K+-medium to Na+-medium, the organism stops protein synthesis, maintains a high rate of RNA synthesis, and increases putrescine synthesis from ornithine manyfold. Under these conditions, the cells do not markedly change their contents of GTP and ppGpp. The proposed mechanism of regulation of RNA and putrescine synthesis by guanine nucleotides does not appear to explain the metabolic phenomena observed in this organism during K+ deficiency. Nevertheless, amino acid depletion in K+-medium does result in a marked increase in ppGpp.