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J Bacteriol, March 1998, p. 1466-1472, Vol. 180, No. 6
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Physiological and Genetic Analyses Leading to Identification of a Biochemical Role for the moeA (Molybdate Metabolism) Gene Product in Escherichia colidagger

Adnan Hasona, Ramesh M. Ray,Dagger and K. T. Shanmugam*

Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611

Received 19 June 1997/Accepted 6 January 1998

A unique class of chlorate-resistant mutants of Escherichia coli which produced formate hydrogenlyase and nitrate reductase activities only when grown in medium with limiting amounts of sulfur compounds was isolated. These mutants failed to produce the two molybdoenzyme activities when cultured in rich medium or glucose-minimal medium. The mutations in these mutants were localized in the moeA gene. Mutant strains with polar mutations in moeA which are also moeB did not produce active molybdoenzymes in any of the media tested. moeA mutants with a second mutation in either cysDNCJI or cysH gene lost the ability to produce active molybdoenzyme even when grown in medium limiting in sulfur compounds. The CysDNCJIH proteins along with CysG catalyze the conversion of sulfate to sulfide. Addition of sulfide to the growth medium of moeA cys double mutants suppressed the MoeA- phenotype. These results suggest that in the absence of MoeA protein, the sulfide produced by the sulfate activation/reduction pathway combines with molybdate in the production of activated molybdenum. Since hydrogen sulfide is known to interact with molybdate in the production of thiomolybdate, it is possible that the MoeA-catalyzed activated molybdenum is a form of thiomolybdenum species which is used in the synthesis of molybdenum cofactor from Mo-free molybdopterin.

* Corresponding author. Mailing address: Department of Microbiology and Cell Science, Box 110700, University of Florida, Gainesville, FL 32611. Phone: (352) 392-2490. Fax: (352) 392-5922. E-mail: shan{at}micro.ifas.ufl.edu.

dagger Florida Agricultural Experiment Station Journal Series no. R06089.

Dagger Present address: Department of Pharmacology and Biophysics, University of Tennessee School of Medicine, Memphis, TN 38163.




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