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Journal of Bacteriology, January 2000, p. 228-232, Vol. 182, No. 1
0021-9193/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Lesions in the nuo Operon, Encoding NADH Dehydrogenase Complex I, Prevent PurF-Independent Thiamine Synthesis and Reduce Flux through the Oxidative Pentose Phosphate Pathway in Salmonella enterica Serovar Typhimurium

Kathy Claas, Shara Weber, and Diana M. Downs*

Department of Bacteriology, University of Wisconsin---Madison, Madison, Wisconsin

Received 19 July 1999/Accepted 13 October 1999

In Salmonella enterica serovar Typhimurium, PurF-independent thiamine synthesis (or alternative pyrimidine biosynthesis) allows strains, under some growth conditions, to synthesize thiamine in the absence of the first step in the purine biosynthetic pathway. Mutations have been isolated in a number of loci that prevent this synthesis and thus result in an Apb- phenotype. Here we identify a new class of mutations that prevent PurF-independent thiamine synthesis and show that they are defective in the nuo genes, which encode the major, energy-generating NADH dehydrogenase of the cell. Data presented here indicated that a nuo mutant has reduced flux through the oxidative pentose phosphate pathway that may contribute to, but is not sufficient to cause, the observed thiamine requirement. We suggest that reduction of the oxidative pentose phosphate pathway capacity in a nuo mutant is an attempt to restore the ratio between reduced and oxidized pyridine nucleotide pools.

* Corresponding author. Mailing address: 1550 Linden Dr., Madison, WI 53711. Phone: (608) 265-4630. Fax: (608) 252-9865. E-mail: downs{at}macc.wisc.edu.

Journal of Bacteriology, January 2000, p. 228-232, Vol. 182, No. 1
0021-9193/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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