Arsenite Oxidase aox Genes from a Metal-Resistant β-Proteobacterium
| Autor: | Marie-Claire Lett, Daniel Muller, Diliana D. Simeonova, Didier Lièvremont, Jean-Claude Hubert |
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| Přispěvatelé: | Dynamique, évolution et expression de génomes de microorganismes (DEEGM), Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2003 |
| Předmět: |
Signal peptide
Transposable element Arsenites Sequence analysis Protein subunit Molecular Sequence Data Genetics and Molecular Biology Microbial Sensitivity Tests MESH: Amino Acid Sequence MESH: Base Sequence Biology Microbiology Arsenic chemistry.chemical_compound Bacterial Proteins Metals Heavy Drug Resistance Bacterial MESH: Arsenic MESH: Drug Resistance Bacterial Amino Acid Sequence MESH: Betaproteobacteria MESH: Bacterial Proteins Molecular Biology Peptide sequence Arsenite MESH: Microbial Sensitivity Tests MESH: Molecular Sequence Data Alcaligenes faecalis Base Sequence Betaproteobacteria Sequence Analysis DNA Periplasmic space MESH: Metals Heavy biology.organism_classification Molecular biology Mutagenesis Insertional [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology MESH: Mutagenesis Insertional MESH: DNA Transposable Elements Biochemistry chemistry DNA Transposable Elements Arsenates MESH: Arsenites Oxidoreductases Oxidation-Reduction MESH: Arsenates |
| Zdroj: | Journal of Bacteriology Journal of Bacteriology, American Society for Microbiology, 2003, 185 (1), pp.135-41 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.185.1.135-141.2003 |
| Popis: | The β-proteobacterial strain ULPAs1, isolated from an arsenic-contaminated environment, is able to efficiently oxidize arsenite [As(III)] to arsenate [As(V)]. Mutagenesis with a lacZ -based reporter transposon yielded two knockout derivatives deficient in arsenite oxidation. Sequence analysis of the DNA flanking the transposon insertions in the two mutants identified two adjacent open reading frames, named aoxA and aoxB , as well as a putative promoter upstream of the aoxA gene. Reverse transcription-PCR data indicated that these genes are organized in an operonic structure. The proteins encoded by aoxA and aoxB share 64 and 72% identity with the small Rieske subunit and the large subunit of the purified and crystallized arsenite oxidase of Alcaligenes faecalis , respectively (P. J. Ellis, T. Conrads, R. Hille, and P. Kuhn, Structure [Cambridge] 9:125-132, 2001). Importantly, almost all amino acids involved in cofactor interactions in both subunits of the A. faecalis enzyme were conserved in the corresponding sequences of strain ULPAs1. An additional Tat (twin-arginine translocation) signal peptide sequence was detected at the N terminus of the protein encoded by aoxA , strongly suggesting that the Tat pathway is involved in the translocation of the arsenite oxidase to its known periplasmic location. |
| Databáze: | OpenAIRE |
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