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Signal transduction protein P(II) is dephosphorylated in Synechocystis sp. strain PCC 6803 by protein phosphatase PphA. To determine the impact of PphA-mediated P(II) dephosphorylation on physiology, the phenotype of a PphA-deficient mutant was analyzed. Mutants lacking either PphA or P(II) were impaired in efficient utilization of nitrate as the nitrogen source. Under conditions of limiting photosystem I (PSI)-reduced ferredoxin, excess reduction of nitrate along with impaired reduction of nitrite occurred in P(II) signaling mutants, resulting in excretion of nitrite to the medium. This effect could be reversed by increasing the level of PSI-reduced ferredoxin. We present evidence that nonphosphorylated P(II) controls the utilization of nitrate in response to low light intensity by tuning down nitrate uptake to meet the actual reduction capacity. This control mechanism can be bypassed by exposing cells to excess levels of nitrate. Uncontrolled nitrate uptake leads to light-dependent nitrite excretion even in wild-type cells, confirming that nitrate uptake controls nitrate utilization in response to limiting photon flux densities.

journal of bacteriology

Signal Transduction Protein P <sub>II</sub> Phosphatase PphA Is Required for Light-Dependent Control of Nitrate Utilization in <i>Synechocystis</i> sp. Strain PCC 6803

Signal Transduction Protein P II Phosphatase PphA Is Required for Light-Dependent Control of Nitrate Utilization in Synechocystis sp. Strain PCC 6803

Signal Transduction Protein P _II Phosphatase PphA Is Required for Light-Dependent Control of Nitrate Utilization in Synechocystis sp. Strain PCC 6803