Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1996 Aug;178(15):4727–4730. doi: 10.1128/jb.178.15.4727-4730.1996

The genes for phosphofructokinase and pyruvate kinase of Lactobacillus delbrueckii subsp. bulgaricus constitute an operon.

P Branny 1, F De La Torre 1, J R Garel 1
PMCID: PMC178247  PMID: 8755908

Abstract

In Lactobacillus delbrueckii subsp. bulgaricus, the pyk gene coding for pyruvate kinase and the pfk gene coding for phosphofructokinase formed a bicistronic operon transcribed into a 2.9-kb RNA. The nucleotide sequence of the pyk gene indicated that the encoded protein possessed an extra C-terminal domain with a potential phosphoenolpyruvate-dependent autophosphorylation site.

Full Text

The Full Text of this article is available as a PDF (276.9 KB).

Selected References

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

  1. Alpert C. A., Frank R., Stüber K., Deutscher J., Hengstenberg W. Phosphoenolpyruvate-dependent protein kinase enzyme I of Streptococcus faecalis: purification and properties of the enzyme and characterization of its active center. Biochemistry. 1985 Feb 12;24(4):959–964. doi: 10.1021/bi00325a023. [DOI] [PubMed] [Google Scholar]
  2. Bairoch A. PROSITE: a dictionary of sites and patterns in proteins. Nucleic Acids Res. 1992 May 11;20 (Suppl):2013–2018. doi: 10.1093/nar/20.suppl.2013. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Branny P., De La Torre F., Garel J. R. Cloning, sequencing, and expression in Escherichia coli of the gene coding for phosphofructokinase in Lactobacillus bulgaricus. J Bacteriol. 1993 Sep;175(17):5344–5349. doi: 10.1128/jb.175.17.5344-5349.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Calzone F. J., Britten R. J., Davidson E. H. Mapping of gene transcripts by nuclease protection assays and cDNA primer extension. Methods Enzymol. 1987;152:611–632. doi: 10.1016/0076-6879(87)52069-9. [DOI] [PubMed] [Google Scholar]
  5. Chevalier C., Saillard C., Bové J. M. Organization and nucleotide sequences of the Spiroplasma citri genes for ribosomal protein S2, elongation factor Ts, spiralin, phosphofructokinase, pyruvate kinase, and an unidentified protein. J Bacteriol. 1990 May;172(5):2693–2703. doi: 10.1128/jb.172.5.2693-2703.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fothergill-Gilmore L. A., Michels P. A. Evolution of glycolysis. Prog Biophys Mol Biol. 1993;59(2):105–235. doi: 10.1016/0079-6107(93)90001-z. [DOI] [PubMed] [Google Scholar]
  7. Fraser C. M., Gocayne J. D., White O., Adams M. D., Clayton R. A., Fleischmann R. D., Bult C. J., Kerlavage A. R., Sutton G., Kelley J. M. The minimal gene complement of Mycoplasma genitalium. Science. 1995 Oct 20;270(5235):397–403. doi: 10.1126/science.270.5235.397. [DOI] [PubMed] [Google Scholar]
  8. Graves M. C., Rabinowitz J. C. In vivo and in vitro transcription of the Clostridium pasteurianum ferredoxin gene. Evidence for "extended" promoter elements in gram-positive organisms. J Biol Chem. 1986 Aug 25;261(24):11409–11415. [PubMed] [Google Scholar]
  9. Hellinga H. W., Evans P. R. Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase. Eur J Biochem. 1985 Jun 3;149(2):363–373. doi: 10.1111/j.1432-1033.1985.tb08934.x. [DOI] [PubMed] [Google Scholar]
  10. Helmann J. D. Compilation and analysis of Bacillus subtilis sigma A-dependent promoter sequences: evidence for extended contact between RNA polymerase and upstream promoter DNA. Nucleic Acids Res. 1995 Jul 11;23(13):2351–2360. doi: 10.1093/nar/23.13.2351. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hueck C. J., Hillen W. Catabolite repression in Bacillus subtilis: a global regulatory mechanism for the gram-positive bacteria? Mol Microbiol. 1995 Feb;15(3):395–401. doi: 10.1111/j.1365-2958.1995.tb02252.x. [DOI] [PubMed] [Google Scholar]
  12. Jetten M. S., Gubler M. E., Lee S. H., Sinskey A. J. Structural and functional analysis of pyruvate kinase from Corynebacterium glutamicum. Appl Environ Microbiol. 1994 Jul;60(7):2501–2507. doi: 10.1128/aem.60.7.2501-2507.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Larsen T. M., Laughlin L. T., Holden H. M., Rayment I., Reed G. H. Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate. Biochemistry. 1994 May 24;33(20):6301–6309. doi: 10.1021/bi00186a033. [DOI] [PubMed] [Google Scholar]
  14. Le Bras G., Deville-Bonne D., Garel J. R. Purification and properties of the phosphofructokinase from Lactobacillus bulgaricus. A non-allosteric analog of the enzyme from Escherichia coli. Eur J Biochem. 1991 Jun 15;198(3):683–687. doi: 10.1111/j.1432-1033.1991.tb16067.x. [DOI] [PubMed] [Google Scholar]
  15. Le Bras G., Garel J. R. Properties of D-lactate dehydrogenase from Lactobacillus bulgaricus: a possible different evolutionary origin for the D- and L-lactate dehydrogenases. FEMS Microbiol Lett. 1991 Mar 15;63(1):89–93. doi: 10.1016/0378-1097(91)90533-g. [DOI] [PubMed] [Google Scholar]
  16. Le Bras G., Garel J. R. Pyruvate kinase from Lactobacillus bulgaricus: possible regulation by competition between strong and weak effectors. Biochimie. 1993;75(9):797–802. doi: 10.1016/0300-9084(93)90130-k. [DOI] [PubMed] [Google Scholar]
  17. Llanos R. M., Harris C. J., Hillier A. J., Davidson B. E. Identification of a novel operon in Lactococcus lactis encoding three enzymes for lactic acid synthesis: phosphofructokinase, pyruvate kinase, and lactate dehydrogenase. J Bacteriol. 1993 May;175(9):2541–2551. doi: 10.1128/jb.175.9.2541-2551.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Moran C. P., Jr, Lang N., LeGrice S. F., Lee G., Stephens M., Sonenshein A. L., Pero J., Losick R. Nucleotide sequences that signal the initiation of transcription and translation in Bacillus subtilis. Mol Gen Genet. 1982;186(3):339–346. doi: 10.1007/BF00729452. [DOI] [PubMed] [Google Scholar]
  19. Muirhead H., Clayden D. A., Barford D., Lorimer C. G., Fothergill-Gilmore L. A., Schiltz E., Schmitt W. The structure of cat muscle pyruvate kinase. EMBO J. 1986 Mar;5(3):475–481. doi: 10.1002/j.1460-2075.1986.tb04236.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Ohara O., Dorit R. L., Gilbert W. Direct genomic sequencing of bacterial DNA: the pyruvate kinase I gene of Escherichia coli. Proc Natl Acad Sci U S A. 1989 Sep;86(18):6883–6887. doi: 10.1073/pnas.86.18.6883. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Reizer J., Hoischen C., Reizer A., Pham T. N., Saier M. H., Jr Sequence analyses and evolutionary relationships among the energy-coupling proteins Enzyme I and HPr of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Protein Sci. 1993 Apr;2(4):506–521. doi: 10.1002/pro.5560020403. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Rosenberg M., Court D. Regulatory sequences involved in the promotion and termination of RNA transcription. Annu Rev Genet. 1979;13:319–353. doi: 10.1146/annurev.ge.13.120179.001535. [DOI] [PubMed] [Google Scholar]
  23. Saier M. H., Jr, Chauvaux S., Deutscher J., Reizer J., Ye J. J. Protein phosphorylation and regulation of carbon metabolism in gram-negative versus gram-positive bacteria. Trends Biochem Sci. 1995 Jul;20(7):267–271. doi: 10.1016/s0968-0004(00)89041-6. [DOI] [PubMed] [Google Scholar]
  24. Sakai H., Ohta T. Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon. Eur J Biochem. 1993 Feb 1;211(3):851–859. doi: 10.1111/j.1432-1033.1993.tb17618.x. [DOI] [PubMed] [Google Scholar]
  25. Speranza M. L., Valentini G., Malcovati M. Fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia coli. Nature of bonds involved in the allosteric mechanism. Eur J Biochem. 1990 Aug 17;191(3):701–704. doi: 10.1111/j.1432-1033.1990.tb19178.x. [DOI] [PubMed] [Google Scholar]
  26. Tanaka K., Sakai H., Ohta T., Matsuzawa H. Molecular cloning of the genes for pyruvate kinase of two bacilli, Bacillus psychrophilus and Bacillus licheniformis, and comparison of the properties of the enzymes produced in Escherichia coli. Biosci Biotechnol Biochem. 1995 Aug;59(8):1536–1542. doi: 10.1271/bbb.59.1536. [DOI] [PubMed] [Google Scholar]
  27. Tinoco I., Jr, Borer P. N., Dengler B., Levin M. D., Uhlenbeck O. C., Crothers D. M., Bralla J. Improved estimation of secondary structure in ribonucleic acids. Nat New Biol. 1973 Nov 14;246(150):40–41. doi: 10.1038/newbio246040a0. [DOI] [PubMed] [Google Scholar]
  28. Triglia T., Peterson M. G., Kemp D. J. A procedure for in vitro amplification of DNA segments that lie outside the boundaries of known sequences. Nucleic Acids Res. 1988 Aug 25;16(16):8186–8186. doi: 10.1093/nar/16.16.8186. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Voskuil M. I., Voepel K., Chambliss G. H. The -16 region, a vital sequence for the utilization of a promoter in Bacillus subtilis and Escherichia coli. Mol Microbiol. 1995 Jul;17(2):271–279. doi: 10.1111/j.1365-2958.1995.mmi_17020271.x. [DOI] [PubMed] [Google Scholar]
  30. Walker D., Chia W. N., Muirhead H. Key residues in the allosteric transition of Bacillus stearothermophilus pyruvate kinase identified by site-directed mutagenesis. J Mol Biol. 1992 Nov 5;228(1):265–276. doi: 10.1016/0022-2836(92)90505-e. [DOI] [PubMed] [Google Scholar]
  31. Weaver R. F., Weissmann C. Mapping of RNA by a modification of the Berk-Sharp procedure: the 5' termini of 15 S beta-globin mRNA precursor and mature 10 s beta-globin mRNA have identical map coordinates. Nucleic Acids Res. 1979 Nov 10;7(5):1175–1193. doi: 10.1093/nar/7.5.1175. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES