Background:In cyanobacteria, starvation-induced phycobilisome degradation is caused by NblA. Results: Synechocystis expresses two NblA proteins that form a heterodimer. The heterodimer binds phycobiliproteins and ClpC and is degraded by a ClpC-ClpP1ClpR protease in vitro. Conclusion: NblA1/NblA2 is an adaptor protein that mediates degradation of phycobilisomes by the ATP-dependent protease ClpC-ClpP1ClpR. Significance: These findings improve our understanding of the mechanisms by which cyanobacteria adapt to changing environmental conditions.

L-Serine is one of the proteinogenic amino acids and participates in several essential processes in all organisms. In plants, the light-dependent photorespiratory and the light-independent phosphoserine pathways contribute to serine biosynthesis. In cyanobacteria, the light-dependent photorespiratory pathway for serine synthesis is well characterized, but the phosphoserine pathway has not been identified. Here, we investigated three candidate genes for enzymes of the phosphoserine pathway in Synechocystis sp. PCC 6803. Only the gene for the D-3-phosphoglycerate dehydrogenase is correctly annotated in the genome database, whereas the 3-phosphoserine transaminase and 3-phosphoserine phosphatase (PSP) proteins are incorrectly annotated and were identified here. All enzymes were obtained as recombinant proteins and showed the activities necessary to catalyse the three-step phosphoserine pathway. The genes coding for the phosphoserine pathway were found in most cyanobacterial genomes listed in CyanoBase. The pathway seems to be essential for cyanobacteria, because it was impossible to mutate the gene coding for PSP in Synechocystis sp. PCC 6803 or in Synechococcus elongatus PCC 7942. A model approach indicates a 30-60 % contribution of the phosphoserine pathway to the overall serine pool. Hence, this study verified that cyanobacteria, similar to plants, use the phosphoserine pathway in addition to photorespiration for serine biosynthesis.

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