This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Johansen, L. E.
Right arrow Articles by Saxild, H. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Johansen, L. E.
Right arrow Articles by Saxild, H. H.
Right arrowPubmed/NCBI databases
*Protein
*Compound via MeSH
*Substance via MeSH
Hazardous Substances DB
*GUANINE

 Previous Article  |  Next Article 

Journal of Bacteriology, September 2003, p. 5200-5209, Vol. 185, No. 17
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.17.5200-5209.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Definition of a Second Bacillus subtilis pur Regulon Comprising the pur and xpt-pbuX Operons plus pbuG, nupG (yxjA), and pbuE (ydhL)

Lars Engholm Johansen,1 Per Nygaard,2 Catharina Lassen,2 Yvonne Agersø,1 and Hans H. Saxild1*

BioCentrum-DTU, Technical University of Denmark, Lyngby,1 Institute of Molecular Biology, Department of Biological Chemistry, University of Copenhagen, Copenhagen, Denmark2

Received 14 March 2003/ Accepted 2 June 2003

In Bacillus subtilis expression of genes or operons encoding enzymes and other proteins involved in purine synthesis is affected by purine bases and nucleosides in the growth medium. The genes belonging to the PurR regulon (purR, purA, glyA, guaC, pbuO, pbuG, and the pur, yqhZ-folD, and xpt-pbuX operons) are controlled by the PurR repressor, which inhibits transcription initiation. Other genes are regulated by a less-well-described transcription termination mechanism that responds to the presence of hypoxanthine and guanine. The pur operon and the xpt-pbuX operon, which were studied here, are regulated by both mechanisms. We isolated two mutants resistant to 2-fluoroadenine in which the pur operon and the xpt-pbuX operon are expressed at increased levels in a PurR-independent manner. The mutations were caused by deletions that disrupted a potential transcription terminator structure located immediately upstream of the ydhL gene. The 5' part of the ydhL leader region contained a 63-nucleotide (nt) sequence very similar to the 5' ends of the leaders of the pur and xpt-pbuX operons. Transcripts of these regions may form a common tandem stem-loop secondary structure. Two additional genes with potential leader regions containing the 63-nt sequence are pbuG, encoding a hypoxanthine-guanine transporter, and yxjA, which was shown to encode a purine nucleoside transporter and is renamed nupG. Transcriptional lacZ fusions and mutations in the 63-nt sequence encoding the possible secondary structures provided evidence that expression of the pur and xpt-pbuX operons and expression of the ydhL, nupG, and pbuG genes are regulated by a common mechanism. The new pur regulon is designated the XptR regulon. Except for ydhL, the operons and genes were negatively regulated by hypoxanthine and guanine. ydhL was positively regulated. The derived amino acid sequence encoded by ydhL (now called pbuE) is similar to the amino acid sequences of metabolite efflux pumps. When overexpressed, PbuE lowers the sensitivity to purine analogs. Indirect evidence indicated that PbuE decreases the size of the internal pool of hypoxanthine. This explains why the hypoxanthine- and guanine-regulated genes are expressed at elevated levels in a mutant that overexpresses pbuE.


* Corresponding author. Mailing address: BioCentrum-DTU, Section for Molecular Microbiology, Technical University of Denmark, Building 301, DK-2800 Lyngby, Denmark. Phone: 45 25 24 95. Fax: 45 88 26 60. E-mail: hhs{at}biocentrum.dtu.dk.


Journal of Bacteriology, September 2003, p. 5200-5209, Vol. 185, No. 17
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.17.5200-5209.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Seif, E., Altman, S. (2008). RNase P cleaves the adenine riboswitch and stabilizes pbuE mRNA in Bacillus subtilis. RNA 14: 1237-1243 [Abstract] [Full Text]  
  • Mulhbacher, J., Lafontaine, D. A. (2007). Ligand recognition determinants of guanine riboswitches. Nucleic Acids Res 0: gkm572v1-13 [Abstract] [Full Text]  
  • Lemay, J.-F., Lafontaine, D. A. (2007). Core requirements of the adenine riboswitch aptamer for ligand binding. RNA 13: 339-350 [Abstract] [Full Text]  
  • Freiberg, C., Brunner, N., Macko, L., Fischer, H. P. (2006). Discovering Antibiotic Efficacy Biomarkers: TOWARD MECHANISM-SPECIFIC HIGH CONTENT COMPOUND SCREENING. Mol. Cell. Proteomics 5: 2326-2335 [Abstract] [Full Text]  
  • Seggewiss, J., Becker, K., Kotte, O., Eisenacher, M., Yazdi, M. R. K., Fischer, A., McNamara, P., Al Laham, N., Proctor, R., Peters, G., Heinemann, M., von Eiff, C. (2006). Reporter Metabolite Analysis of Transcriptional Profiles of a Staphylococcus aureus Strain with Normal Phenotype and Its Isogenic hemB Mutant Displaying the Small-Colony-Variant Phenotype. J. Bacteriol. 188: 7765-7777 [Abstract] [Full Text]  
  • Mijakovic, I., Petranovic, D., Macek, B., Cepo, T., Mann, M., Davies, J., Jensen, P. R., Vujaklija, D. (2006). Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine. Nucleic Acids Res 34: 1588-1596 [Abstract] [Full Text]  
  • Schyns, G., Potot, S., Geng, Y., Barbosa, T. M., Henriques, A., Perkins, J. B. (2005). Isolation and Characterization of New Thiamine-Deregulated Mutants of Bacillus subtilis. J. Bacteriol. 187: 8127-8136 [Abstract] [Full Text]  
  • Nygaard, P., Saxild, H. H. (2005). The Purine Efflux Pump PbuE in Bacillus subtilis Modulates Expression of the PurR and G-Box (XptR) Regulons by Adjusting the Purine Base Pool Size. J. Bacteriol. 187: 791-794 [Abstract] [Full Text]