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Effector specificity mutants of the transcriptional activator NahR of naphthalene degrading Pseudomonas define protein sites involved in binding of aromatic inducers

Opened Access Effector specificity mutants of the transcriptional activator NahR of naphthalene degrading Pseudomonas define protein sites involved in binding of aromatic inducers

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Autor: Cebolla, Ángel
Sousa Martín, Carolina
Lorenzo, Víctor de
Departamento: Universidad de Sevilla. Departamento de Microbiología y Parasitología
Fecha: 1997
Publicado en: Journal of Biological Chemistry, 272 (7), 3986-3992.
Tipo de documento: Artículo
Resumen: This work reports a genetic analysis of the interactions between NahR, the LysR-type regulator of the NAH operons for biodegradation of naphthalene in Pseudomonas, and its aromatic effectors. Six mutants encoding NahR variants responsive to salicylate analogs such as benzoate, which is not an inducer for the wild type regulator, were isolated with a polymerase chain reactionbased saturation mutagenesis protocol. Most mutants displaying a specific change of effector profile bore single amino acid substitutions within a short protein segment of 60 residues located at the central portion of the NahR sequence. Some of the protein variants exhibited an increased affinity for salicylate and also for otherwise suboptimal effectors, with apparent Ks * values 5–100-fold lower than those of the wild type NahR protein. In addition, all mutants were activated by inducers bearing novel substituents at positions 1 or 2 of the aromatic ring and displayed also an enhanced tolerance ...
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Cita: Cebolla, Á., Sousa Martín, C. y Lorenzo, V.d. (1997). Effector specificity mutants of the transcriptional activator NahR of naphthalene degrading Pseudomonas define protein sites involved in binding of aromatic inducers. Journal of Biological Chemistry, 272 (7), 3986-3992.
Tamaño: 265.2Kb
Formato: PDF

URI: http://hdl.handle.net/11441/41988

DOI: 10.1074/jbc.272.7.3986

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