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J. Bacteriol. doi:10.1128/JB.00252-08
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Extracytoplasmic processes impaired by inactivation of trxA (thioredoxin gene) in Bacillus subtilis

Mirja Carlsson Möller and Lars Hederstedt*

* To whom correspondence should be addressed. Email: Lars.Hederstedt{at}cob.lu.se.


   Abstract

The trxA gene is regarded essential in Bacillus subtilis but the roles of the TrxA protein in this gram-positive bacterium are largely unknown. Inactivation of trxA results in deoxyribonucleoside and cysteine or methionine auxotrophy. This phenotype is as expected if the TrxA protein is important for activity of the class Ib ribonucleotide reductase and adenosine-5'-phosphosulfate/3'-phosphoadenosine-5'-phophosulfate reductase. We demonstrate that TrxA-deficiency in addition causes defects in endospore and cytochrome c synthesis. These effects were suppressed by BdbD-deficiency indicating that TrxA in the cytoplasm is the primary electron donor to several different thiol-disulfide oxidoreductases active on the outer side of the B. subtilis cytoplasmic membrane.







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