| Summary: | <p>Abstract</p> <p>Background</p> <p>The <it>dspA </it>(<it>hik33</it>) gene, coding for a putative sensory histidine kinase, is conserved in plastids (<it>ycf26</it>) and cyanobacteria. It has been linked with a number of different stress responses in cyanobacteria.</p> <p>Results</p> <p>We constructed an insertional mutant of <it>dspA </it>(<it>ycf26) </it>in <it>Synechocystis </it>6803. We found little phenotypic effect during nitrogen starvation. However, when the mutation was combined with deletion of the <it>pta </it>gene coding for phosphotransacetylase, a more significant phenotype was observed. Under nitrogen starvation, the <it>pta/dspA </it>double mutant degrades its phycobilisomes less than the wild type and still has about half of its chlorophyll-protein complexes.</p> <p>Conclusion</p> <p>Our data indicates that acetyl-phosphate-dependent phosphorylation of response regulator(s) overlaps with DspA-dependent signalling of the degradation of chlorophyll-protein complexes (and to a lesser extent phycobilisomes) in <it>Synechocystis </it>6803.</p>
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