Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1985 Nov;164(2):816–822. doi: 10.1128/jb.164.2.816-822.1985

Role of glnB and glnD gene products in regulation of the glnALG operon of Escherichia coli.

R Bueno, G Pahel, B Magasanik
PMCID: PMC214324  PMID: 2865248

Abstract

We have isolated insertion and deletion mutants in glnB, the structural gene of PII, a member of the adenylylation system for glutamine synthetase of Escherichia coli, to study the role of PII in the regulation of the synthesis of glutamine synthetase and of histidase in response to nitrogen deprivation or excess. We have studied the effects of this mutation alone and combined with null mutations resulting from the insertion of transposons or from a deletion in the other genes affecting this regulation, glnD, glnF (ntrA), glnG (ntrC), and glnL (ntrB). Our results confirm that only the products of glnF and glnG are essential for this regulation. In cells of the wild type, the response is mediated by the products of glnD and glnB via the product of glnL. In the condition of nitrogen excess, PII, the product of glnB, appears to convert the product of glnL to a form that prevents the activation of transcription of the structural genes for glutamine synthetase and for histidase by the products of glnF and glnG. During nitrogen deprivation, uridylyltransferase, the product of glnD, is activated by the intracellular excess of 2-ketoglutarate over glutamine and converts PII to PII-UMP and changes the form of the glnL product to one that stimulates the activation of transcription of glutamine synthetase and histidase by the products of glnF and glnG.

Full text

PDF
816

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bachmann B. J. Linkage map of Escherichia coli K-12, edition 7. Microbiol Rev. 1983 Jun;47(2):180–230. doi: 10.1128/mr.47.2.180-230.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Backman K., Chen Y. M., Magasanik B. Physical and genetic characterization of the glnA--glnG region of the Escherichia coli chromosome. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3743–3747. doi: 10.1073/pnas.78.6.3743. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bancroft S., Rhee S. G., Neumann C., Kustu S. Mutations that alter the covalent modification of glutamine synthetase in Salmonella typhimurium. J Bacteriol. 1978 Jun;134(3):1046–1055. doi: 10.1128/jb.134.3.1046-1055.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Berg D. E., Davies J., Allet B., Rochaix J. D. Transposition of R factor genes to bacteriophage lambda. Proc Natl Acad Sci U S A. 1975 Sep;72(9):3628–3632. doi: 10.1073/pnas.72.9.3628. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bloom F. R., Levin M. S., Foor F., Tyler B. Regulation of glutamine synthetase formation in Escherichia coli: characterization of mutants lacking the uridylyltransferase. J Bacteriol. 1978 May;134(2):569–577. doi: 10.1128/jb.134.2.569-577.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Brown M. S., Segal A., Stadtman E. R. Modulation of glutamine synthetase adenylylation and deadenylylation is mediated by metabolic transformation of the P II -regulatory protein. Proc Natl Acad Sci U S A. 1971 Dec;68(12):2949–2953. doi: 10.1073/pnas.68.12.2949. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Casadaban M. J., Cohen S. N. Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: in vivo probe for transcriptional control sequences. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4530–4533. doi: 10.1073/pnas.76.9.4530. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Chen Y. M., Backman K., Magasanik B. Characterization of a gene, glnL, the product of which is involved in the regulation of nitrogen utilization in Escherichia coli. J Bacteriol. 1982 Apr;150(1):214–220. doi: 10.1128/jb.150.1.214-220.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Foor F., Cedergren R. J., Streicher S. L., Rhee S. G., Magasanik B. Glutamine synthetase of Klebsiella aerogenes: properties of glnD mutants lacking uridylyltransferase. J Bacteriol. 1978 May;134(2):562–568. doi: 10.1128/jb.134.2.562-568.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Foor F., Reuveny Z., Magasanik B. Regulation of the synthesis of glutamine synthetase by the PII protein in Klebsiella aerogenes. Proc Natl Acad Sci U S A. 1980 May;77(5):2636–2640. doi: 10.1073/pnas.77.5.2636. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. MacNeil T., Roberts G. P., MacNeil D., Tyler B. The products of glnL and glnG are bifunctional regulatory proteins. Mol Gen Genet. 1982;188(2):325–333. doi: 10.1007/BF00332696. [DOI] [PubMed] [Google Scholar]
  12. Magasanik B. Genetic control of nitrogen assimilation in bacteria. Annu Rev Genet. 1982;16:135–168. doi: 10.1146/annurev.ge.16.120182.001031. [DOI] [PubMed] [Google Scholar]
  13. Merrick M. J. Nitrogen control of the nif regulon in Klebsiella pneumoniae: involvement of the ntrA gene and analogies between ntrC and nifA. EMBO J. 1983;2(1):39–44. doi: 10.1002/j.1460-2075.1983.tb01377.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Pahel G., Rothstein D. M., Magasanik B. Complex glnA-glnL-glnG operon of Escherichia coli. J Bacteriol. 1982 Apr;150(1):202–213. doi: 10.1128/jb.150.1.202-213.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Pahel G., Tyler B. A new glnA-linked regulatory gene for glutamine synthetase in Escherichia coli. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4544–4548. doi: 10.1073/pnas.76.9.4544. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Pahel G., Zelenetz A. D., Tyler B. M. gltB gene and regulation of nitrogen metabolism by glutamine synthetase in Escherichia coli. J Bacteriol. 1978 Jan;133(1):139–148. doi: 10.1128/jb.133.1.139-148.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Prival M. J., Brenchley J. E., Magasanik B. Glutamine synthetase and the regulation of histidase formation in Klebsiella aerogenes. J Biol Chem. 1973 Jun 25;248(12):4334–4344. [PubMed] [Google Scholar]
  18. Reitzer L. J., Magasanik B. Expression of glnA in Escherichia coli is regulated at tandem promoters. Proc Natl Acad Sci U S A. 1985 Apr;82(7):1979–1983. doi: 10.1073/pnas.82.7.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Reuveny Z., Foor F., Magasanik B. Regulation of glutamine synthetase by regulatory protein PII in Klebsiella aerogenes mutants lacking adenylyltransferase. J Bacteriol. 1981 May;146(2):740–745. doi: 10.1128/jb.146.2.740-745.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Rothstein D. M., Pahel G., Tyler B., Magasanik B. Regulation of expression from the glnA promoter of Escherichia coli in the absence of glutamine synthetase. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7372–7376. doi: 10.1073/pnas.77.12.7372. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Ueno-Nishio S., Backman K. C., Magasanik B. Regulation at the glnL-operator-promoter of the complex glnALG operon of Escherichia coli. J Bacteriol. 1983 Mar;153(3):1247–1251. doi: 10.1128/jb.153.3.1247-1251.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Ueno-Nishio S., Mango S., Reitzer L. J., Magasanik B. Identification and regulation of the glnL operator-promoter of the complex glnALG operon of Escherichia coli. J Bacteriol. 1984 Oct;160(1):379–384. doi: 10.1128/jb.160.1.379-384.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Wanner B. L., Wieder S., McSharry R. Use of bacteriophage transposon Mu d1 to determine the orientation for three proC-linked phosphate-starvation-inducible (psi) genes in Escherichia coli K-12. J Bacteriol. 1981 Apr;146(1):93–101. doi: 10.1128/jb.146.1.93-101.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Winans S. C., Elledge S. J., Krueger J. H., Walker G. C. Site-directed insertion and deletion mutagenesis with cloned fragments in Escherichia coli. J Bacteriol. 1985 Mar;161(3):1219–1221. doi: 10.1128/jb.161.3.1219-1221.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES