Structural highlights
FunctionA0A031LR83_9GAMM Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414] Publication Abstract from PubMedAcinetobacter 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 A, 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.,Steimbruch BA, Sartorio MG, Cortez N, Albanesi D, Lisa MN, Repizo GD Sci Rep. 2022 Mar 12;12(1):4321. doi: 10.1038/s41598-022-08052-z. PMID:35279679[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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