Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
4359263 | Research in Microbiology | 2009 | 9 Pages |
Abstract
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.
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Authors
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,