Extracytoplasmic processes impaired by inactivation of trxA (thioredoxin gene) in Bacillus subtilis.
The trxA gene is regarded as 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 expected if the TrxA protein is important for the activity of the class Ib ribonucleotide reductase and adenosine-5'-phosphosulfate/3'-phosphoadenosine-5'-phosphosulfate reductase. We demonstrate here that a 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.
Möller
Mirja Carlsson
MC
Department of Cell and Organism Biology, Lund University, Sölvegatan 35, SE-223 62 Lund, Sweden.
Hederstedt
Lars
L
D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D003545:Cysteine / Q000378:metabolism; D045304:Cytochromes c / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D008954:Models, Biological; D009154:Mutation; D013696:Temperature; D013879:Thioredoxins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*
D001426:Bacterial Proteins; D013879:Thioredoxins; D045304:Cytochromes c; D003545:Cysteine