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Journal of Bacteriology, September 2001, p. 5426-5430, Vol. 183, No. 18
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.18.5426-5430.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

CotA of Bacillus subtilis Is a Copper-Dependent Laccase

Marie-Françoise Hullo, Ivan Moszer, Antoine Danchin, and Isabelle Martin-Verstraete*

Unité de Génétique des Génomes Bactériens, Institut Pasteur, 75724 Paris Cedex 15, France

Received 31 October 2000/Accepted 13 June 2001

The spore coat protein CotA of Bacillus subtilis displays similarities with multicopper oxidases, including manganese oxidases and laccases. B. subtilis is able to oxidize manganese, but neither CotA nor other sporulation proteins are involved. We demonstrate that CotA is a laccase. Syringaldazine, a specific substrate of laccases, reacted with wild-type spores but not with Delta cotA spores. CotA may participate in the biosynthesis of the brown spore pigment, which appears to be a melanin-like product and to protect against UV light.

* Corresponding author. Mailing address: Unité de Génétique des Génomes Bactériens, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France. Phone: 33 1 45 68 72 95. Fax: 33 1 45 68 89 48. E-mail: iverstra{at}pasteur.fr.

Journal of Bacteriology, September 2001, p. 5426-5430, Vol. 183, No. 18
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.18.5426-5430.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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