ABC transporter slr0982 affects response of Synechocystis sp. PCC 6803 to oxidative stress caused by methyl viologen

The exposure of methyl viologen (a bipyridine salt) can lead to the production of reactive oxygen species, causing oxidative stress to organisms. ABC transporters have been reported to be involved in multi-drug resistance and have a role in MV detoxification. Here, we performed a protein structure simulation of the Slr0982 protein encoding ABC transporters, and confirmed that the region from Phe57 to Gln257 was the ABC transporter-type domain of the Slr0982 protein. The results of protein sequence alignment showed that Slr0982 protein was similar to Slr2108 protein (polysialic acid transport ATP-binding protein) and Slr0354 protein (ABC transporter). We reported that the mutation of slr0982 reduced the tolerance of Synechocystis sp. PCC 6803 to oxidative stress induced by methyl viologen. The deletion of slr0982 reduced the ability of cells to resist oxidative stress. Our data confirmed that the deletion of slr0982 could affect the concentration of exopolysaccharide and the expression of some genes related to carbohydrate metabolism, thus decreasing polysaccharide transport. Importantly, the exogenous addition of exopolysaccharide extracted from wild type can effectively reduce the oxidative damage to Δslr0982 by methyl viologen. This study expands the role of ABC transporters in MV-induced oxidative stress and provides an insight into the further analysis of the response of cyanobacteria to oxidative stress.