Autor: |
López Maury, Luis
Sánchez Riego, Ana María Reyes Rosa, José Carlos Florencio Bellido, Francisco Javier |
Departamento: | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular |
Fecha: | 2009 |
Publicado en: | Journal of Bacteriology, 191 (11), 3534-3543. |
Tipo de documento: | Artículo |
Resumen: |
Arsenic resistance in Synechocystis sp. strain PCC 6803 is mediated by an operon of three genes in which arsC codes for an arsenate reductase with unique characteristics. Here we describe the identification of two additional and nearly identical genes coding for arsenate reductases in Synechocystis sp. strain PCC 6803, which we have designed arsI1 and arsI2, and the biochemical characterization of both ArsC (arsenate reductase) and ArsI. Functional analysis of single, double, and triple mutants shows that both ArsI enzymes are active arsenate reductases but that their roles in arsenate resistance are essential only in the absence of ArsC. Based on its biochemical properties, ArsC belongs to a family that, though related to thioredoxin-dependent arsenate reductases, uses the glutathione/glutaredoxin system for reduction, whereas ArsI belongs to the previously known glutaredoxin-dependent family. We have also analyzed the role in arsenate resistance of the three glutaredoxins present in... [Ver más] |
Cita: | López Maury, L., Sánchez Riego, A.M., Reyes Rosa, J.C. y Florencio Bellido, F.J. (2009). The glutathione/glutaredoxin system is essential for arsenate reduction in Synechocystis sp. strain PCC 6803. Journal of Bacteriology, 191 (11), 3534-3543. |
URI: http://hdl.handle.net/11441/62908
DOI: 10.1128/JB.01798-08
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