Abstract/Summary

Mutation of ptsP encoding EINtr of the PTSNtr system in Rhizobium leguminosarum strain Rlv3841 caused a pleiotropic phenotype as observed with many bacteria. The mutant formed dry colonies and grew poorly on organic nitrogen or dicarboxylates. Most strikingly the ptsP mutant had low activity of a broad range of ATP-dependent ABC transporters. This lack of activation, which occurred post-translationally, may explain many of the pleiotropic effects. In contrast proton-coupled transport systems were not inhibited in a ptsP mutant. Regulation by PtsP also involves two copies of ptsN that code for EIIANtr, resulting in a phosphorylation cascade. As in Escherichia coli, the Rlv3841 PTSNtr system also regulates K+ homeostasis by transcriptional activation of the high-affinity ATP-dependent K+ transporter KdpABC. This involves direct interaction of a two-component sensor regulator pair KdpDE with unphosphorylated EIIANtr. Critically, ptsP mutants, which cannot phosphorylate PtsN1 or PtsN2, had a fully activated KdpABC transporter. This is the opposite pattern from that observed with ABC transporters which apparently require phosphorylation of PtsN. These results suggest that ATP-dependent transport might be regulated via PTSNtr responding to the cellular energy charge. ABC transport may be inactivated at low energy charge, conserving ATP for essential processes including K+ homeostasis.