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Novel AB-type antioxidant protein in the symbiotic bacterium Sinorhizobium meliloti.
Free oxygen radicals from dissolved molecular oxygen and hydrogen peroxide have been implicated in the breakdown of DNA, proteins and lipids, causing oxidative damage to DNA, and membrane proteins and lipids, respectively. Many symbiotic Rhizobia, including Sinorhizobium meliloti, can produce oxygen radicals during the process of nitrogen fixation. We have reported the presence of a protein that is highly thermostable, with antioxidant activity, and could be classified as a new type of antioxidant protein (AB protein). This study aimed to investigate the distribution of the AB protein in S. meliloti strains, to explore the biosynthesis, biochemical characteristics and structure of the AB protein, and to investigate the roles of this protein in the free oxygen radical metabolism of S. meliloti. The AB protein was demonstrated to be a novel AB type protein. The AB protein was constitutively expressed in all S. meliloti strains and was not detected in cells during exponential growth. The levels of the AB protein were regulated by different nitrogen sources. The metabolic pathway of the AB protein was similar to that of Gpx, an established antioxidant protein from other bacteria. The deduced amino acid sequence of the AB protein showed a high degree of similarity to Gpx proteins. The AB protein was located in the periplasmic region of the cell and is likely to be secreted into the periplasm. On exposure to oxygen radicals generated by the reaction between hydrogen peroxide and potassium ferricyanide, the AB protein could protect the S. meliloti cells from damage. The results presented in this study suggest that the AB protein could be considered as an important structural protein and a novel antioxidant protein that may play a role in protecting cells from oxidative damage.In vivo cellular accumulation and

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