1887

Abstract

The gene encodes an 84 amino acid reading frame; in it is positioned between the and genes of the purine biosynthetic operon. Disruption of resulted in a purine-auxotrophic phenotype. When was expressed it was able to complement a mutation. Growth experiments and enzyme analysis of mutant strains revealed a defective phosphoribosylformylglycinamidine synthetase (FGAM synthetase). In the organisms in which FGAM synthetase has been studied a single polypeptide is responsible for activity. In some organisms two separate genes – in the and genes – encode polypeptides with similarity to the N-terminal and the C-terminal region, respectively, of the single-polypeptide FGAM synthetase. Thus, active FGAM synthetase in requires the gene product in addition to the and gene products. Open reading frames with sequence similarity to are found in other Gram-positive organisms, in a cyanobacterium and in methanogenic archaea. The designation is proposed for this novel function in purine biosynthesis in .

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-146-4-807
2000-04-01
2024-04-19
Loading full text...

Full text loading...

/deliver/fulltext/micro/146/4/1460807a.html?itemId=/content/journal/micro/10.1099/00221287-146-4-807&mimeType=html&fmt=ahah

References

  1. Barnes T. S., Bleskan J. H., Hart I. M., Walton K. A., Barton J. W., Patterson D. 1994; Purification of, generation of monoclonal antibodies to, and mapping of phosphoribosyl N-formylglycine amidotransferase. Biochemistry 33:1850–1860 [CrossRef]
    [Google Scholar]
  2. Birnboim H. C., Doly J. 1979; A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res 7:1513–1523 [CrossRef]
    [Google Scholar]
  3. Borriss R., Porwollik S., Schroeter R. 1996; The 52°–55° segment of the Bacillus subtilis chromosome: a region devoted to purine uptake and metabolism, and containing the genes cotA, pabP and guaA and the pur gene cluster within a 34960 bp nucleotide sequence. Microbiology 142:3027–3031 [CrossRef]
    [Google Scholar]
  4. Boylan R. J., Mendelson N. H., Brooks D., Young F. E. 1972; Regulation of the bacterial cell wall: analysis of a mutant of Bacillus subtilis defective in biosynthesis of teichoic acid. J Bacteriol 110:281–290
    [Google Scholar]
  5. Christiansen L. C., Schou S., Nygaard P., Saxild H. H. 1997; Xanthine metabolism in Bacillus subtilis: characterization of the xpt–pbuX operon and evidence for purine- and nitrogen-controlled expression of genes involved in xanthine salvage and catabolism. J Bacteriol 179:2540–2550
    [Google Scholar]
  6. Ebbole D. J., Zalkin H. 1987; Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide biosynthesis. J Biol Chem 262:8274–8287
    [Google Scholar]
  7. Ebbole D. J., Zalkin H. 1989; Bacillus subtilis pur operon expression and regulation. J Bacteriol 171:2136–2141
    [Google Scholar]
  8. Hanahan D. 1983; Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166:557–580 [CrossRef]
    [Google Scholar]
  9. Houlberg U., Hove-Jensen B., Jochimsen B., Nygaard P. 1983; Identification of the enzymatic reactions encoded by the purG and purI genes of Escherichia coli. J Bacteriol 154:1485–1488
    [Google Scholar]
  10. Jensen K. F., Houlberg U., Nygaard P. 1979; Thin-layer chromotographic methods to isolate 32P-labeled 5-phosphoribosyl-α-1-pyrophosphate (PRPP): determination of cellular PRPP pools and assay of PRPP synthetase activity. Anal Biochem 98:254–263 [CrossRef]
    [Google Scholar]
  11. Kunst F., Ogasawara N., Moszer I.148 other authors 1997; The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature 390:249–256 [CrossRef]
    [Google Scholar]
  12. Miller J. H. 1972; Assay of β-galactosidase. In Experiments in Molecular Genetics pp. 352–355Edited by Miller J. H. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  13. Peltonen T., Mäntsälä P. 1999; Isolation and characterization of a purC(orf)QLF operon from Lactobacillus lactis MG1614. Mol Gen Genet 261:31–41 [CrossRef]
    [Google Scholar]
  14. Saxild H. H., Nygaard P. 1987; Genetic and physiological characterization of Bacillus subtilis mutants resistant to purine analogs. J Bacteriol 169:2977–2983
    [Google Scholar]
  15. Saxild H. H., Nygaard P. 1988; Gene–enzyme relationships of the purine biosynthetic pathway in Bacillus subtilis. Mol Gen Genet 211:160–167 [CrossRef]
    [Google Scholar]
  16. Saxild H. H., Nygaard P. 1991; Regulation of levels of purine biosynthetic enzymes in Bacillus subtilis: effects of changing nucleotide pools. J Gen Microbiol 137:2387–2394 [CrossRef]
    [Google Scholar]
  17. Saxild H. H., Jacobsen J. H., Nygaard P. 1994; Genetic and physiological characterization of a formate-dependent 5′-phosphoribosyl-1-glycinamide transformylase activity in Bacillus subtilis. Mol Gen Genet 242:415–420
    [Google Scholar]
  18. Saxild H. H., Andersen L. N., Hammer K. 1996; dra–nupC–pdp operon of Bacillus subtilis: nucleotide sequence, induction by deoxyribonucleosides, and transcriptional regulation by the deoR-encoded DeoR repressor protein. J Bacteriol 178:424–434
    [Google Scholar]
  19. Schendel F. J., Mueller E., Stubbe J., Shiau A., Smith J. M. 1989; Formylglycinamide ribonucleotide synthetase from Escherichia coli: cloning, sequencing, overproduction, isolation, and characterization. Biochemistry 28:2459–2471 [CrossRef]
    [Google Scholar]
  20. Vagner V., Dervyn E., Ehrlich D. 1998; A vector for systematic gene inactivation in Bacillus subtilis. Microbiology 144:3097–3104 [CrossRef]
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-146-4-807
Loading
/content/journal/micro/10.1099/00221287-146-4-807
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error