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Journal of Bacteriology, October 2000, p. 5332-5341, Vol. 182, No. 19
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Purine Catabolism in Escherichia coli and Function of Xanthine Dehydrogenase in Purine Salvage

Hualin Xi,dagger Barbara L. Schneider,Dagger and Larry Reitzer*

Department of Molecular and Cell Biology, The University of Texas at Dallas, Richardson, Texas 75083-0688

Received 20 March 2000/Accepted 4 July 2000

Escherichia coli is not known to utilize purines, other than adenine and adenosine, as nitrogen sources. We reinvestigated purine catabolism because a computer analysis suggested several potential sigma 54-dependent promoters within a 23-gene cluster whose products have homology to purine catabolic enzymes. Our results did not provide conclusive evidence that the sigma 54-dependent promoters are active. Nonetheless, our results suggest that some of the genes are metabolically significant. We found that even though several purines did not support growth as the sole nitrogen source, they did stimulate growth with aspartate as the nitrogen source. Cells produced 14CO2 from minimal medium containing [14C]adenine, which implies allantoin production. However, neither ammonia nor carbamoyl phosphate was produced, which implies that purine catabolism is incomplete and does not provide nitrogen during nitrogen-limited growth. We constructed strains with deletions of two genes whose products might catalyze the first reaction of purine catabolism. Deletion of one eliminated 14CO2 production from [14C]adenine, which implies that its product is necessary for xanthine dehydrogenase activity. We changed the name of this gene to xdhA. The xdhA mutant grew faster with aspartate as a nitrogen source. The mutant also exhibited sensitivity to adenine, which guanosine partially reversed. Adenine sensitivity has been previously associated with defective purine salvage resulting from impaired synthesis of guanine nucleotides from adenine. We propose that xanthine dehydrogenase contributes to this purine interconversion.

* Corresponding author. Mailing address: Department of Molecular and Cell Biology, Mail Station FO 3.1, The University of Texas at Dallas, P.O. Box 830688, Richardson, TX 75083-0688. Phone: (972) 883-2502/2523. Fax: (972) 883-2409. E-mail: reitzer{at}utdallas.edu.

dagger Present address: Cereon Genomics, Cambridge, MA 02139.

Dagger Present address: Department of Biology, University of California at San Diego, La Jolla, CA 92093-0116.

Journal of Bacteriology, October 2000, p. 5332-5341, Vol. 182, No. 19
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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