A <Emphasis Type="Italic">Synechococcus elongatus</Emphasis> PCC 7942 mutant with a higher tolerance toward the herbicide bentazone also confers resistance to sodium chloride stress

Following a N-methyl-N'-nitro-N-nitrosoguanidine-based mutagenesis of Synechococcus elongatus PCC 7942 wild type, we were able to select several mutants with an enhanced tolerance toward the herbicide bentazone (3-isopropyl-1H-2,1,3-benzothiadiazine-4(3H)-one 2,2-dioxide). Mutant Mu1 has in part been previously characterized. In the present paper we report on another mutant, called Mu2, which also has a higher tolerance toward bentazone. Since Mu2 showed a better growth than WT when cultivated with elevated NaCl concentrations in the growth medium and since S. elongatus WT has previously been classified to be low salt tolerant, we were especially interested in the identification of the modifications conferring this higher salt tolerance to mutant Mu2. Immunoblot analyses provided evidence that Mu2 had a constitutively higher expression of PsbO and of IsiA. In addition, in Mu2 a significantly higher concentration of IdiA was detected under salt stress as compared to WT. These three proteins most likely contribute to a better protection and/or stabilization of photosystem II. Moreover, Mu2 had a higher amount of the photosystem I reaction center proteins PsaAB under salt stress than WT. In addition, the amount of the ferredoxin:NADP+ oxidoreductase and also of the ATP synthase was constitutively higher in Mu2 than in WT. In contrast to WT the latter two proteins did not decrease under salt stress in Mu2. Therefore, it can be assumed that Mu2 could maintain a high cyclic electron transport activity around photosystem I under salt stress. It can be assumed that the combination of these modifications of the electron transport chain cause a better protection of photosystem II against oxidative damage and cause an increase of cyclic electron transport activity around photosystem I with ATP synthesis. Thus, the overall cellular energization in Mu2 relative to WT is improved. Together with putative other not yet identified modifications this seems to enable Mu2 to energize its cytoplasmic membrane-localized ion pumps more effectively than WT and, as a consequence, to keep the intracellular NaCl concentration low.