Characterization of a new periplasmic single-domain rhodanese encoded by a sulfur-regulated gene in a hyperthermophilic bacterium Aquifex aeolicus |
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Authors: | Marie-Cé cile Giuliani,Cé cile Jourlin-Castelli,Gisè le Leroy,Aderrahman Hachani,Marie Thé rè se Giudici-Orticoni |
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Affiliation: | 1. Laboratoire de Bioénergétique et Ingénierie des Protéines (BIP), IMM-CNRS, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, France;2. Laboratoire de Chimie Bactérienne (LCB), IMM-CNRS, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, France;3. Laboratoire d''Ingénierie des Systèmes Macromoléculaires (LISM), IMM-CNRS, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, France;4. Imperial College London, Division of Cell and Molecular Biology, Center for Molecular Microbiology and Infection, South Kensington Campus, Flowers Building, SW7 2AZ London, United Kingdom |
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Abstract: | Rhodaneses (thiosulfate cyanide sulfurtransferases) are enzymes involved in the production of the sulfur in sulfane form, which has been suggested to be the relevant biologically active sulfur species. Rhodanese domains occur in the three major domains of life. We have characterized a new periplasmic single-domain rhodanese from a hyperthermophile bacterium, Aquifex aeolicus, with thiosulfate:cyanide transferase activity, Aq-1599. The oligomeric organization of the enzyme is stabilized by a disulfide bridge. To date this is the first characterization from a hyperthermophilic bacterium of a periplasmic sulfurtransferase with a disulfide bridge. The aq-1599 gene belongs to an operon that also contains a gene for a prepilin peptidase and that is up-regulated when sulfur is used as electron acceptor. Finally, we have observed a sulfur-dependent bacterial adherence linked to an absence of flagellin suggesting a possible role for sulfur detection by A. aeolicus. |
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Keywords: | Aquifex aeolicus Sulfurtransferase Hyperthermophile |
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