Journal
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Volume 75, Issue 16, Pages 5209-5217Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.00888-09
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Funding
- National Science Foundation
- Department of Energy
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Shewanella oneidensis MR-1, a facultatively anaerobic gammaproteobacterium, respires a variety of anaerobic terminal electron acceptors, including the inorganic sulfur compounds sulfite (SO32-), thiosulfate (S2O32-), tetrathionate (S4O62-), and elemental sulfur (S-0). The molecular mechanism of anaerobic respiration of inorganic sulfur compounds by S. oneidensis, however, is poorly understood. In the present study, we identified a three-gene cluster in the S. oneidensis genome whose translated products displayed 59 to 73% amino acid similarity to the products of phsABC, a gene cluster required for S-0 and S2O32- respiration by Salmonella enterica serovar Typhimurium LT2. Homologs of phsA (annotated as psrA) were identified in the genomes of Shewanella strains that reduce S-0 and S2O32- yet were missing from the genomes of Shewanella strains unable to reduce these electron acceptors. A new suicide vector was constructed and used to generate a markerless, in-frame deletion of psrA, the gene encoding the putative thiosulfate reductase. The psrA deletion mutant (PSRA1) retained expression of downstream genes psrB and psrC but was unable to respire S-0 or S2O32- as the terminal electron acceptor. Based on these results, we postulate that PsrA functions as the main subunit of the S. oneidensis S2O32- terminal reductase whose end products (sulfide [HS-] or SO32-) participate in an intraspecies sulfur cycle that drives S-0 respiration.
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