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Journal of Bacteriology, January 2005, p. 601-610, Vol. 187, No. 2
0021-9193/05/$08.00+0     doi:10.1128/JB.187.2.601-610.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Roles of Thioredoxin Reductase during the Aerobic Life of Lactococcus lactis

Karin Vido,1 Hélène Diemer,2 Alain Van Dorsselaer,2 Emmanuelle Leize,2 Vincent Juillard,1 Alexandra Gruss,1 and Philippe Gaudu1*

Unité de Recherches Laitières et Génétique Appliquée, INRA, Domaine de Vilvert, Jouy en Josas,1 Laboratoire de Spectrométrie de Masse Bio-Organique, CNRS UMR 7509, ECPM, Université Louis Pasteur de Strasbourg, Strasbourg, France2

Received 27 July 2004/ Accepted 24 September 2004

Thiol-disulfide bond balance is generally maintained in bacteria by thioredoxin reductase-thioredoxin and/or glutathione-glutaredoxin systems. Some gram-positive bacteria, including Lactococcus lactis, do not produce glutathione, and the thioredoxin system is presumed to be essential. We constructed an L. lactis trxB1 mutant. The mutant was obtained under anaerobic conditions in the presence of dithiothreitol (DTT). Unexpectedly, the trxB1 mutant was viable without DTT and under aerated static conditions, thus disproving the essentiality of this system. Aerobic growth of the trxB1 mutant did not require glutathione, also ruling out the need for this redox maintenance system. Proteomic analyses showed that known oxidative stress defense proteins are induced in the trxB1 mutant. Two additional effects of trxB1 were not previously reported in other bacteria: (i) induction of proteins involved in fatty acid or menaquinone biosynthesis, indicating that membrane synthesis is part of the cellular response to a redox imbalance, and (ii) alteration of the isoforms of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GapB). We determined that the two GapB isoforms in L. lactis differed by the oxidation state of catalytic-site cysteine C152. Unexpectedly, a decrease specific to the oxidized, inactive form was observed in the trxB1 mutant, possibly because of proteolysis of oxidized GapB. This study showed that thioredoxin reductase is not essential in L. lactis and that its inactivation triggers induction of several mechanisms acting at the membrane and metabolic levels. The existence of a novel redox function that compensates for trxB1 deficiency is suggested.

* Corresponding author. Mailing address: Unité de Recherches Laitières et Génétique Appliquée, INRA, Domaine de Vilvert, 78352 Jouy en Josas, France. Phone: 33 1 34 65 20 80. Fax: 33 1 34 65 20 65. E-mail: gaudu{at}diamant.jouy.inra.fr.

Journal of Bacteriology, January 2005, p. 601-610, Vol. 187, No. 2
0021-9193/05/$08.00+0     doi:10.1128/JB.187.2.601-610.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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