Cloning, purification and characterization of Geobacillus stearothermophilus V uroporphyrinogen-III C-methyltransferase: evaluation of its role in resistance to potassium tellurite in Escherichia coli

Manuel A. Araya, Juan C. Tantaleán, José M. Pérez, Derie E. Fuentes, Iván L. Calderón, Claudia P. Saavedra, Radhika Burra, Thomas G. Chasteen, Claudio C. Vásquez

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

7 Citas (Scopus)

Resumen

The Geobacillus stearothermophilus V cobA gene encoding uroporphyrinogen-III C-methyltransferase (also referred to as SUMT) was cloned into Escherichia coli and the recombinant enzyme was overexpressed and purified to homogeneity. The enzyme binds S-adenosyl-l-methionine and catalyzes the production of III methyl uroporphyrinogen in vitro. E. coli cells expressing the G. stearothermophilus V cobA gene exhibited increased resistance to potassium tellurite and potassium tellurate. Site-directed mutagenesis of cobA abolished tellurite resistance of the mesophilic, heterologous host and SUMT activity in vitro. No methylated, volatile derivatives of tellurium were found in the headspace of tellurite-exposed cobA-expressing E. coli, suggesting that the role of SUMT methyltransferase in tellurite(ate) detoxification is not related to tellurium volatilization.

Idioma originalInglés
Páginas (desde-hasta)125-133
Número de páginas9
PublicaciónResearch in Microbiology
Volumen160
N.º2
DOI
EstadoPublicada - mar 2009

Áreas temáticas de ASJC Scopus

  • Microbiología
  • Biología molecular

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