The products of the isiAB operon are a chlorophyll antenna protein (IsiA) and flavodoxin (IsiB), which accumulate in cyanobacteria grown under iron starvation conditions. Here we show that strong light triggers de-repression of isiAB transcription and leads to IsiA and flavodoxin accumulation under iron replete conditions. Genetic deletion of isiAB resulted in a photosensitive phenotype, with accumulation of reactive oxygen species and cell bleaching in high light, while the flavodoxin-deficient isiB null mutant expressing isiA was phototolerant. We conclude that IsiA protects cyanobacteria from photooxidative stress. IsiA is the first example of a chlorophyll antenna protein outside the extended LHC family that is induced transiently by high light and that fulfills a photoprotective role.
We establish here that iron deficiency causes oxidative stress in the cyanobacterium Anabaena sp. strain PCC 7120. Iron starvation leads to a significant increase in reactive oxygen species, whose effect can be abolished by treatment with the antioxidant tempol (4-hydroxy-2,2,6,6-tetramethylpiperidine 1-oxyl). Oxidative stress induced by iron starvation could be a common feature of photosynthetic bacteria.
Mutations in a gene, stpA, had been correlated with the loss of tolerance to high NaCl concentrations in the cyanobacterium Synechocystis sp. strain PCC 6803. Genetic, biochemical, and physiological evidence shows that stpA encodes glucosylglycerol-phosphate phosphatase. stpA mutants are salt sensitive and accumulate glucosylglycerol-phosphate, the precursor of the osmoprotectant glucosylglycerol necessary for salt adaptation of Synechocystis. The consensus motif present in acid phosphatases was found in StpA; however, the homology with other sugar phosphatases is very poor. The amount of stpA mRNA was increased by growth of the cells in the presence of NaCl concentrations above 170 mM. Expression of stpA in Escherichia coli allowed the production of a 46-kDa protein which exhibited glucosylglycerol-phosphate phosphatase activity. The StpAspecific antibody revealed a protein of similar size in extracts of Synechocystis, and the amount of this protein was increased in salt-adapted cells. The protein produced in E. coli had lost the requirement for activation by NaCl that was observed for the genuine cyanobacterial enzyme.
When the filamentous cyanobacterium Anabaena PCC 7120 is exposed to combined nitrogen starvation, 5 to 10% of the cells along each filament at semiregular intervals differentiate into heterocysts specialized in nitrogen fixation. Heterocysts are terminally differentiated cells in which the major cell division protein FtsZ is undetectable. In this report, we provide molecular evidence indicating that cell division is necessary for heterocyst development. FtsZ, which is translationally fused to the green fluorescent protein (GFP) as a reporter, is found to form a ring structure at the mid-cell position. SulA from Escherichia coli inhibits the GTPase activity of FtsZ in vitro and prevents the formation of FtsZ rings when expressed in Anabaena PCC 7120. The expression of sulA arrests cell division and suppresses heterocyst differentiation completely. The antibiotic aztreonam, which is targeted to the FtsI protein necessary for septum formation, has similar effects on both cell division and heterocyst differentiation, although in this case, the FtsZ ring is still formed. Therefore, heterocyst differentiation is coupled to cell division but independent of the formation of the FtsZ ring. Consistently, once the inhibitory pressure of cell division is removed, cell division should take place first before heterocyst differentiation resumes at a normal frequency. The arrest of cell division does not affect the accumulation of 2-oxoglutarate, which triggers heterocyst differentiation. Consistently, a nonmetabolizable analogue of 2-oxoglutarate does not rescue the failure of heterocyst differentiation when cell division is blocked. These results suggest that the control of heterocyst differentiation by cell division is independent of the 2-oxoglutarate signal.
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