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Characterization of an alcohol dehydrogenase from the cyanobacterium Synechocystis sp. strain PCC 6803 that responds to environmental stress conditions via the Hik34-Rre1 two-component system

Opened Access Characterization of an alcohol dehydrogenase from the cyanobacterium Synechocystis sp. strain PCC 6803 that responds to environmental stress conditions via the Hik34-Rre1 two-component system

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Autor: Vidal Vidal, Rebeca
López Maury, Luis
García Guerrero, Miguel
Florencio Bellido, Francisco Javier
Departamento: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular
Fecha: 2009
Publicado en: Journal of Bacteriology, 191 (13), 4383-4391.
Tipo de documento: Artículo
Resumen: The slr1192 (adhA) gene from Synechocystis sp. strain PCC 6803 encodes a member of the medium-chain alcohol dehydrogenase/reductase family. The gene product AdhA exhibits NADP-dependent alcohol dehydrogenase activity, acting on a broad variety of aromatic and aliphatic primary alcohols and aldehydes but not on secondary alcohols or ketones. It exhibits superior catalytic efficiency for aldehyde reduction compared to that for alcohol oxidation. The enzyme is a cytosolic protein present in photoautotrophically grown Synechocystis cells. The expression of AdhA is enhanced upon the exposure of cells to different environmental stresses, although it is not essential for survival even under such stress conditions. The induction of the expression of the adhA gene is dependent on the Hik34-Rre1 two-component system, as it is severely impaired in mutant strains lacking either the histidine kinase Hik34 or the response regulator Rre1. In vitro DNA-protein interaction analysis reveals that the re...
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Cita: Vidal Vidal, R., López Maury, L., García Guerrero, M. y Florencio Bellido, F.J. (2009). Characterization of an alcohol dehydrogenase from the cyanobacterium Synechocystis sp. strain PCC 6803 that responds to environmental stress conditions via the Hik34-Rre1 two-component system. Journal of Bacteriology, 191 (13), 4383-4391.
Tamaño: 1.432Mb
Formato: PDF

URI: http://hdl.handle.net/11441/62906

DOI: 10.1128/JB.00183-09

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