- THIS ARTICLE
- Full Text (PDF)
- Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Similar articles in this journal
- Similar articles in PubMed
- Alert me to new issues of the journal
- Download to citation manager
- Reprints & Permissions
- CITING ARTICLES
- Citing Articles via HighWire
- Citing Articles via Google Scholar
- GOOGLE SCHOLAR
- Articles by Zilles, J. L.
- Articles by Downs, D. M.
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Zilles, J. L.
- Articles by Downs, D. M.
Genetics, Vol 144, 883-892, Copyright © 1996
INVESTIGATIONS |
A Novel Involvement of the PurG and PurI Proteins in Thiamine Synthesis Via the Alternative Pyrimidine Biosynthetic (APB) Pathway in Salmonella typhimurium
J. L. Zilles and D. M. Downs
Department of Bacteriology, University of Wisconsin, Madison, Wisconsin 53706
Thiamine is thought to be synthesized by two alternative pathways, one involving the first four enzymes of the purine pathway and a second that can function independently of the purine pathway. Insertion mutations in purG and purI prevent thiamine synthesis through the alternative pyrimidine biosynthetic (APB) pathway under aerobic but not anaerobic growth conditions. In contrast, point mutations in purG and purI caused one of three distinct phenotypes: Pur(-) Apb(-), Pur(-) Apb(+), or Pur(+) Apb(-). Analysis of these three mutant classes demonstrated two genetically separable functions for PurG and PurI in thiamine synthesis. In addition to their known enzymatic role in de novo purine synthesis, we propose that PurG and PurI play a novel, possibly nonenzymatic role in the APB pathway. Suppression analysis of Pur(-) Apb(-) mutants identified two new genetic loci involved in the APB pathway, apbB and apbD. We show here that mutations in apbB and apbD cause distinct, allele-specific suppression of the thiamine requirement of purG and purI mutants. Our results suggest that PurG and PurI and one or more components of the APB pathway may function as a complex needed for aerobic function of the APB pathway.
This article has been cited by other articles:
 |
|
 |
|
  M. J. Koenigsknecht, I. Ramos, and D. M. Downs Glutamine Phosphoribosylpyrophosphate Amidotransferase-independent Phosphoribosyl Amine Synthesis from Ribose 5-Phosphate and Glutamine or Asparagine J. Biol. Chem., September 28, 2007; 282(39): 28379 - 28384. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G. R. Bjork and K. Nilsson 1-Methylguanosine-Deficient tRNA of Salmonella enterica Serovar Typhimurium Affects Thiamine Metabolism J. Bacteriol., February 1, 2003; 185(3): 750 - 759. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Allen, J. L. Zilles, and D. M. Downs Metabolic Flux in Both the Purine Mononucleotide and Histidine Biosynthetic Pathways Can Influence Synthesis of the Hydroxymethyl Pyrimidine Moiety of Thiamine in Salmonella enterica J. Bacteriol., November 15, 2002; 184(22): 6130 - 6137. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. L. Zilles, T. J. Kappock, J. Stubbe, and D. M. Downs Altered Pathway Routing in a Class of Salmonella enterica Serovar Typhimurium Mutants Defective in Aminoimidazole Ribonucleotide Synthetase J. Bacteriol., April 1, 2001; 183(7): 2234 - 2240. [Abstract] [Full Text]
|
|
|
|
|
|
J. L. Enos-Berlage and D. M. Downs Biosynthesis of the Pyrimidine Moiety of Thiamine Independent of the PurF Enzyme (Phosphoribosylpyrophosphate Amidotransferase) in Salmonella typhimurium: Incorporation of Stable Isotope-Labeled Glycine and Formate J. Bacteriol., February 1, 1999; 181(3): 841 - 848. [Abstract] [Full Text]
|
|