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Journal of Bacteriology, August 1999, p. 4509-4516, Vol. 181, No. 15
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Characterization of an Atypical Superoxide Dismutase from Sinorhizobium meliloti

Renata Santos,1 Stephane Bocquet,2,dagger Alain Puppo,3 and Danièle Touati1,*

Laboratoire de Génétique Moléculaire des Réponses Adaptatives1 and Laboratoire d'Embryologie Moléculaire,2 Institut Jacques Monod, CNRS-Universités Paris 6 et 7, 75251 Paris Cedex 05, and Laboratoire de Biologie Végétale et Microbiologie, CNRS ERS 590, Université de Nice Sophia-Antipolis, 06108 Nice Cedex 02,3 France

Received 11 January 1999/Accepted 24 May 1999

Sinorhizobium meliloti Rm5000 is an aerobic bacterium that can live free in the soil or in symbiosis with the roots of leguminous plants. A single detectable superoxide dismutase (SOD) was found in free-living growth conditions. The corresponding gene was isolated from a genomic library by using a sod fragment amplified by PCR from degenerate primers as a probe. The sodA gene was located in the chromosome. It is transcribed monocistronically and encodes a 200-amino-acid protein with a theoretical Mr of 22,430 and pI of 5.8. S. meliloti SOD complemented a deficient E. coli mutant, restoring aerobic growth of a sodA sodB recA strain, when the gene was expressed from the synthetic tac promoter but not from its own promoter. Amino acid sequence alignment showed great similarity with Fe-containing SODs (FeSODs), but the enzyme was not inactivated by H2O2. The native enzyme was purified and found to be a dimeric protein, with a specific activity of 4,000 U/mg. Despite its Fe-type sequence, atomic absorption spectroscopy showed manganese to be the cofactor (0.75 mol of manganese and 0.24 mol of iron per mol of monomer). The apoenzyme was prepared from crude extracts of S. meliloti. Activity was restored by dialysis against either MnCl2 or Fe(NH4)2(SO4)2, demonstrating the cambialistic nature of the S. meliloti SOD. The recovered activity with manganese was sevenfold higher than with iron. Both reconstituted enzymes were resistant to H2O2. Sequence comparison with 70 FeSODs and MnSODs indicates that S. meliloti SOD contains several atypical residues at specific sites that might account for the activation by manganese and resistance to H2O2 of this unusual Fe-type SOD.

* Corresponding author. Mailing address: Laboratoire de Génétique Moléculaire des Réponses Adaptatives, Institut Jacques Monod, 2 place Jussieu, 75251 Paris Cedex 05, France. Phone: 33 1 44274719. Fax: 33 1 44277667. E-mail: touatida{at}ccr.jussieu.fr.

dagger Present address: Institut de Génétique Humaine, 34396 Montpellier Cedex 5, France.

Journal of Bacteriology, August 1999, p. 4509-4516, Vol. 181, No. 15
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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