A role for the signal transduction protein PII in the control of nitrate/nitrite uptake in a cyanobacterium

In the cyanobacterium Synechococcus sp. strain PCC 7942, ammonium exerts a rapid and reversible inhibition of the nitrate and nitrite uptake, and the P-II protein (GlnB) is differentially phosphorylated depending on the intracellular NIC balance. RNA/DNA hybridizations, as well as nitrate and nitrite uptake experiments, were carried out with the wild-type strain and a P-II-null mutant. The transcriptional control by ammonium of the expression of the nir-nrtABCD-narB operon remained operative in the mutant but, in contrast to the wild-type strain, the mutant took up nitrate and nitrite even in the presence of ammonium. Moreover, the mild-type phenotype was restored by insertion of a copy of the wild-type glnB gene in the genome of the P-II-null mutant. These results indicate that the unphosphorylated form of P-II is involved in the short-term inhibition by ammonium of the nitrate and nitrite uptake in Synechococcus sp, strain PCC 7942. (C) 1998 Federation of European Biochemical Societies.