Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1987 Aug;169(8):3539–3545. doi: 10.1128/jb.169.8.3539-3545.1987

Identification of endogenous inducers of the mal regulon in Escherichia coli.

M Ehrmann, W Boos
PMCID: PMC212430  PMID: 3038842

Abstract

The expression of the maltose regulon in Escherichia coli is induced when maltose or maltodextrins are present in the growth medium. Mutations in malK, which codes for a component of the transport system, result in the elevated expression of the remaining mal genes. Uninduced expression in the wild type, as well as elevated expression in malK mutants, is strongly repressed at high osmolarity. In the absence of malQ-encoded amylomaltase, expression remains high at high osmolarity. We found that uninduced expression in the wild type and elevated expression in malK mutants were paralleled by the appearance of two types of endogenous carbohydrates. One, produced primarily at high osmolarity, was identified as comprising maltodextrins that are derived from glycogen or glycogen-synthesizing enzymes. The other, produced primarily at low osmolarity, consisted of an oligosaccharide that was not derived from glycogen. We isolated a mutant that no longer synthesized this oligosaccharide. The gene carrying this mutation, termed malI, was mapped at min 36 on the E. coli linkage map. A Tn10 insertion in malI also resulted in the loss of constitutivity at low osmolarity and delayed the induction of the maltose regulon by exogenous inducers.

Full text

PDF
3542

Images in this article

3542Image
on p.3542

Selected References

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

  1. Alphen W. V., Lugtenberg B. Influence of osmolarity of the growth medium on the outer membrane protein pattern of Escherichia coli. J Bacteriol. 1977 Aug;131(2):623–630. doi: 10.1128/jb.131.2.623-630.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ames G. F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu Rev Biochem. 1986;55:397–425. doi: 10.1146/annurev.bi.55.070186.002145. [DOI] [PubMed] [Google Scholar]
  3. Bochner B. R., Huang H. C., Schieven G. L., Ames B. N. Positive selection for loss of tetracycline resistance. J Bacteriol. 1980 Aug;143(2):926–933. doi: 10.1128/jb.143.2.926-933.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bohin J. P., Kennedy E. P. Mapping of a locus (mdoA) that affects the biosynthesis of membrane-derived oligosaccharides in Escherichia coli. J Bacteriol. 1984 Mar;157(3):956–957. doi: 10.1128/jb.157.3.956-957.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Brass J. M. The cell envelope of gram-negative bacteria: new aspects of its function in transport and chemotaxis. Curr Top Microbiol Immunol. 1986;129:1–92. doi: 10.1007/978-3-642-71399-6_1. [DOI] [PubMed] [Google Scholar]
  6. Bremer E., Silhavy T. J., Weinstock G. M. Transposable lambda placMu bacteriophages for creating lacZ operon fusions and kanamycin resistance insertions in Escherichia coli. J Bacteriol. 1985 Jun;162(3):1092–1099. doi: 10.1128/jb.162.3.1092-1099.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Bukau B., Ehrmann M., Boos W. Osmoregulation of the maltose regulon in Escherichia coli. J Bacteriol. 1986 Jun;166(3):884–891. doi: 10.1128/jb.166.3.884-891.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Casadaban M. J. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol. 1976 Jul 5;104(3):541–555. doi: 10.1016/0022-2836(76)90119-4. [DOI] [PubMed] [Google Scholar]
  9. Chapon C. Role of the catabolite activator protein in the maltose regulon of Escherichia coli. J Bacteriol. 1982 May;150(2):722–729. doi: 10.1128/jb.150.2.722-729.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Débarbouillé M., Shuman H. A., Silhavy T. J., Schwartz M. Dominant constitutive mutations in malT, the positive regulator gene of the maltose regulon in Escherichia coli. J Mol Biol. 1978 Sep 15;124(2):359–371. doi: 10.1016/0022-2836(78)90304-2. [DOI] [PubMed] [Google Scholar]
  11. Freundlieb S., Boos W. Alpha-amylase of Escherichia coli, mapping and cloning of the structural gene, malS, and identification of its product as a periplasmic protein. J Biol Chem. 1986 Feb 25;261(6):2946–2953. [PubMed] [Google Scholar]
  12. Gilson E., Rousset J. P., Charbit A., Perrin D., Hofnung M. malM, a new gene of the maltose regulon in Escherichia coli K12. I. malM is the last gene of the malK-lamB operon and encodes a periplasmic protein. J Mol Biol. 1986 Oct 5;191(3):303–311. doi: 10.1016/0022-2836(86)90127-0. [DOI] [PubMed] [Google Scholar]
  13. Govons S., Vinopal R., Ingraham J., Preiss J. Isolation of mutants of Escherichia coli B altered in their ability to synthesize glycogen. J Bacteriol. 1969 Feb;97(2):970–972. doi: 10.1128/jb.97.2.970-972.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Gowrishankar J. Identification of osmoresponsive genes in Escherichia coli: evidence for participation of potassium and proline transport systems in osmoregulation. J Bacteriol. 1985 Oct;164(1):434–445. doi: 10.1128/jb.164.1.434-445.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Grothe S., Krogsrud R. L., McClellan D. J., Milner J. L., Wood J. M. Proline transport and osmotic stress response in Escherichia coli K-12. J Bacteriol. 1986 Apr;166(1):253–259. doi: 10.1128/jb.166.1.253-259.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Hatfield D., Hofnung M., Schwartz M. Genetic analysis of the maltose A region in Escherichia coli. J Bacteriol. 1969 May;98(2):559–567. doi: 10.1128/jb.98.2.559-567.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Hatfield D., Hofnung M., Schwartz M. Nonsense mutations in the maltose A region of the genetic map of Escherichia coli. J Bacteriol. 1969 Dec;100(3):1311–1315. doi: 10.1128/jb.100.3.1311-1315.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Hengge R., Boos W. Maltose and lactose transport in Escherichia coli. Examples of two different types of concentrative transport systems. Biochim Biophys Acta. 1983 Aug 11;737(3-4):443–478. doi: 10.1016/0304-4157(83)90009-6. [DOI] [PubMed] [Google Scholar]
  19. Kennedy E. P. Osmotic regulation and the biosynthesis of membrane-derived oligosaccharides in Escherichia coli. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1092–1095. doi: 10.1073/pnas.79.4.1092. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Kleckner N., Barker D. F., Ross D. G., Botstein D. Properties of the translocatable tetracycline-resistance element Tn10 in Escherichia coli and bacteriophage lambda. Genetics. 1978 Nov;90(3):427–461. doi: 10.1093/genetics/90.3.427. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. May G., Faatz E., Villarejo M., Bremer E. Binding protein dependent transport of glycine betaine and its osmotic regulation in Escherichia coli K12. Mol Gen Genet. 1986 Nov;205(2):225–233. doi: 10.1007/BF00430432. [DOI] [PubMed] [Google Scholar]
  22. Measures J. C. Role of amino acids in osmoregulation of non-halophilic bacteria. Nature. 1975 Oct 2;257(5525):398–400. doi: 10.1038/257398a0. [DOI] [PubMed] [Google Scholar]
  23. Munro G. F., Bell C. A., Lederman M. Multiple transport components for putrescine in Escherichia coli. J Bacteriol. 1974 Jun;118(3):952–963. doi: 10.1128/jb.118.3.952-963.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Munro G. F., Bell C. A. Polyamine requirements of a conditional polyamine auxotroph of Escherichia coli. J Bacteriol. 1973 Aug;115(2):469–475. doi: 10.1128/jb.115.2.469-475.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Munro G. F., Hercules K., Morgan J., Sauerbier W. Dependence of the putrescine content of Escherichia coli on the osmotic strength of the medium. J Biol Chem. 1972 Feb 25;247(4):1272–1280. [PubMed] [Google Scholar]
  26. Munro G. F., Sauerbier W. Osmotically induced excretion of putrescine by mutants of Escherichia coli defective in potassium transport. J Bacteriol. 1973 Oct;116(1):488–490. doi: 10.1128/jb.116.1.488-490.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Müller N., Heine H. G., Boos W. Characterization of the Salmonella typhimurium mgl operon and its gene products. J Bacteriol. 1985 Jul;163(1):37–45. doi: 10.1128/jb.163.1.37-45.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Perroud B., Le Rudulier D. Glycine betaine transport in Escherichia coli: osmotic modulation. J Bacteriol. 1985 Jan;161(1):393–401. doi: 10.1128/jb.161.1.393-401.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Reyes M., Treptow N. A., Shuman H. A. Transport of p-nitrophenyl-alpha-maltoside by the maltose transport system of Escherichia coli and its subsequent hydrolysis by a cytoplasmic alpha-maltosidase. J Bacteriol. 1986 Mar;165(3):918–922. doi: 10.1128/jb.165.3.918-922.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Robbins A. R., Guzman R., Rotman B. Roles of individual mgl gene products in the beta-methylgalactoside transport system of Escherichia coli K12. J Biol Chem. 1976 May 25;251(10):3112–3116. [PubMed] [Google Scholar]
  31. Rousset J. P., Gilson E., Hofnung M. malM, a new gene of the maltose regulon in Escherichia coli K12. II. Mutations affecting the signal peptide of the MalM protein. J Mol Biol. 1986 Oct 5;191(3):313–320. doi: 10.1016/0022-2836(86)90128-2. [DOI] [PubMed] [Google Scholar]
  32. Shuman H. A., Silhavy T. J. Identification of the malK gene product. A peripheral membrane component of the Escherichia coli maltose transport system. J Biol Chem. 1981 Jan 25;256(2):560–562. [PubMed] [Google Scholar]

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

RESOURCES