查看文章

PTS^Ntr is a regulatory phosphotransferase system in many bacteria. Mutation of the PTS^Ntr enzymes causes pleiotropic growth phenotypes, dry colony morphology and a posttranslational inactivation of ABC transporters in Rhizobium leguminosarum 3841. The PTS^Ntr proteins EI^Ntr and 2 copies of EIIA^Ntr have been described previously. Here we identify the intermediate phosphocarrier protein NPr and show its phosphorylation by EI^Ntr in vitro. Furthermore we demonstrate that phosphorylation of EI^Ntr and NPr is required for ABC transport activation and that the N-terminal GAF domain of EI^Ntr is not required for autophosphorylation. Previous studies have shown that non-phosphorylated EIIA^Ntr is able to modulate the transcriptional activation of the high affinity potassium transporter KdpABC. In R. leguminosarum 3841 kdpABC expression strictly depends on EIIA^Ntr. Here we demonstrate that under strong potassium limitation ABC transport is inactivated, presumably by non-phosphorylated EIIA^Ntr. This is to our knowledge the first report where PTS^Ntr dictates an essential cellular function. This is achieved by the inverse regulation of two important ATP dependent transporter classes.