Abstract
A response regulator, NblR, of the cyanobacterium Synechococcus elongatus PCC 7942 is known to induce expression of the nblA gene, a key factor in phycobilisome degradation (bleaching) under nutrient-deprivation conditions. In this study, we observed phosphorylation-independent regulation of NblR activity. We constructed a mutant strain expressing NblR (D57A), in which a putative phospho-accepting Asp-57 was replaced with Ala residue. Under nitrogen deprivation, this strain exhibited the typical bleaching phenotype observed in wild-type cells. Moreover, in the mutant, the nblA transcript accumulated at a level similar to that of the wild type. Our results indicate that activation of NblR is independent of phosphorylation, if any, by a cognate histidine kinase. Screening of proteins interacting with NblR by yeast two-hybrid analysis revealed two candidates, MreC and NarB, suggesting a novel mechanism that activates NblR, or other functions of the response regulator.
