| Summary: | <p>Abstract</p> <p>Background</p> <p>Polyamine synthesis produces methylthioadenosine, which has to be disposed of. The cell recycles it into methionine through methylthioribose (MTR). Very little was known about MTR recycling for methionine salvage in <it>Bacillus subtilis</it>.</p> <p>Results</p> <p>Using <it>in silico</it> genome analysis and transposon mutagenesis in <it>B. subtilis</it> we have experimentally uncovered the major steps of the dioxygen-dependent methionine salvage pathway, which, although similar to that found in <it>Klebsiella pneumoniae</it>, recruited for its implementation some entirely different proteins. The promoters of the genes have been identified by primer extension, and gene expression was analyzed by Northern blotting and <it>lacZ</it> reporter gene expression. Among the most remarkable discoveries in this pathway is the role of an analog of ribulose diphosphate carboxylase (Rubisco, the plant enzyme used in the Calvin cycle which recovers carbon dioxide from the atmosphere) as a major step in MTR recycling.</p> <p>Conclusions</p> <p>A complete methionine salvage pathway exists in <it>B. subtilis</it>. This pathway is chemically similar to that in <it>K. pneumoniae</it>, but recruited different proteins to this purpose. In particular, a paralogue or Rubisco, MtnW, is used at one of the steps in the pathway. A major observation is that in the absence of MtnW, MTR becomes extremely toxic to the cell, opening an unexpected target for new antimicrobial drugs. In addition to methionine salvage, this pathway protects <it>B. subtilis</it> against dioxygen produced by its natural biotope, the surface of leaves (phylloplane).</p>
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