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Journal of Bacteriology, September 1999, p. 5876-5879, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Cloning and Characterization of a Sulfonate/alpha -Ketoglutarate Dioxygenase from Saccharomyces cerevisiae

Deborah A. Hogan,1,2 Thomas A. Auchtung,2 and Robert P. Hausinger1,2,3,*

Center for Microbial Ecology1 and Departments of Microbiology2 and Biochemistry,3 Michigan State University, East Lansing, Michigan 48824

Received 19 February 1999/Accepted 13 July 1999

The Saccharomyces cerevisiae open reading frame YLL057c is predicted to encode a gene product with 31.5% amino acid sequence identity to Escherichia coli taurine/alpha -ketoglutarate dioxygenase and 27% identity to Ralstonia eutropha TfdA, a herbicide-degrading enzyme. Purified recombinant yeast protein is shown to be an Fe(II)-dependent sulfonate/alpha -ketoglutarate dioxygenase. Although taurine is a poor substrate, a variety of other sulfonates are utilized, with the best natural substrates being isethionate and taurocholate. Disruption of the gene encoding this enzyme negatively affects the use of isethionate and taurine as sulfur sources by S. cerevisiae, providing strong evidence that YLL057c plays a role in sulfonate catabolism.

* Corresponding author. Mailing address: Department of Microbiology, 160 Giltner Hall, Michigan State University, East Lansing, MI 48824. Phone: (517) 353-9675. Fax: (517) 353-8957. E-mail: hausinge{at}pilot.msu.edu.

Journal of Bacteriology, September 1999, p. 5876-5879, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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