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Acinetobacter sp.  Ver3 is a polyextremophilic strain characterized by a high tolerance to radiation and pro-oxidants. The Ver3 genome comprises the  sodB  and  sodC  genes encoding an iron ( AV3 SodB) and a copper/zinc superoxide dismutase ( AV3 SodC), respectively; however, the specific role(s) of these genes has remained elusive. We show that the expression of  sodB  remained unaltered in different oxidative stress conditions whereas  sodC  was up-regulated in the presence of blue light. Besides, we studied the changes in the in vitro activity of each SOD enzyme in response to diverse agents and solved the crystal structure of  AV3 SodB at 1.34 Å, one of the highest resolutions achieved for a SOD. Cell fractionation studies interestingly revealed that  AV3 SodB is located in the cytosol whereas  AV3 SodC is also found in the periplasm. Consistently, a bioinformatic analysis of the genomes of 53  Acinetobacter  species pointed out the presence of at least one SOD type in each compartment, suggesting that these enzymes are separately required to cope with oxidative stress. Surprisingly,  AV3 SodC was found in an active state also in outer membrane vesicles, probably exerting a protective role. Overall, our multidisciplinary approach highlights the relevance of SOD enzymes when  Acinetobacter  spp . are confronted with oxidizing agents.

The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3