Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1987 Nov;169(11):5333–5335. doi: 10.1128/jb.169.11.5333-5335.1987

Efficient utilization and operation of the gluconate-inducible system of the promoter of the Bacillus subtilis gnt operon in Escherichia coli.

Y Miwa 1, Y Fujita 1
PMCID: PMC213950  PMID: 3117776

Abstract

A DNA fragment containing the promoter of the Bacillus subtilis gluconate (gnt) operon and its first gene (gntR) was cloned into Escherichia coli. E. coli recognized this promoter efficiently and precisely. Moreover, the gluconate-inducible system of this operon operated even in E. coli.

Full text

PDF
5333

Images in this article

5334Image
on p.5334
5335Image
on p.5335

Selected References

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

  1. Aiba H., Adhya S., de Crombrugghe B. Evidence for two functional gal promoters in intact Escherichia coli cells. J Biol Chem. 1981 Nov 25;256(22):11905–11910. [PubMed] [Google Scholar]
  2. Berk A. J., Sharp P. A. Sizing and mapping of early adenovirus mRNAs by gel electrophoresis of S1 endonuclease-digested hybrids. Cell. 1977 Nov;12(3):721–732. doi: 10.1016/0092-8674(77)90272-0. [DOI] [PubMed] [Google Scholar]
  3. Fujita Y., Fujita T. Genetic analysis of a pleiotropic deletion mutation (delta igf) in Bacillus subtilis. J Bacteriol. 1983 May;154(2):864–869. doi: 10.1128/jb.154.2.864-869.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fujita Y., Fujita T. Identification and nucleotide sequence of the promoter region of the Bacillus subtilis gluconate operon. Nucleic Acids Res. 1986 Feb 11;14(3):1237–1252. doi: 10.1093/nar/14.3.1237. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Fujita Y., Fujita T., Miwa Y., Nihashi J., Aratani Y. Organization and transcription of the gluconate operon, gnt, of Bacillus subtilis. J Biol Chem. 1986 Oct 15;261(29):13744–13753. [PubMed] [Google Scholar]
  6. Fujita Y., Fujita T. The gluconate operon gnt of Bacillus subtilis encodes its own transcriptional negative regulator. Proc Natl Acad Sci U S A. 1987 Jul;84(13):4524–4528. doi: 10.1073/pnas.84.13.4524. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Fujita Y., Nihashi J., Fujita T. The characterization and cloning of a gluconate (gnt) operon of Bacillus subtilis. J Gen Microbiol. 1986 Jan;132(1):161–169. doi: 10.1099/00221287-132-1-161. [DOI] [PubMed] [Google Scholar]
  8. Horinouchi S., Weisblum B. Nucleotide sequence and functional map of pE194, a plasmid that specifies inducible resistance to macrolide, lincosamide, and streptogramin type B antibodies. J Bacteriol. 1982 May;150(2):804–814. doi: 10.1128/jb.150.2.804-814.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kaempfer R. O., Magasanik B. Effect of infection with T-even phage on the inducible synthesis of beta-glactosidase in Escherichia coli. J Mol Biol. 1967 Aug 14;27(3):453–468. doi: 10.1016/0022-2836(67)90051-4. [DOI] [PubMed] [Google Scholar]
  10. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  11. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  12. Tullis R. H., Rubin H. Calcium protects DNase I from proteinase K: a new method for the removal of contaminating RNase from DNase I. Anal Biochem. 1980 Sep 1;107(1):260–264. doi: 10.1016/0003-2697(80)90519-9. [DOI] [PubMed] [Google Scholar]

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

RESOURCES