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. 1984 Jul;159(1):93–99. doi: 10.1128/jb.159.1.93-99.1984

Transposon Tn10-dependent expression of the lamB gene in Escherichia coli.

J M Brass, M D Manson, T J Larson
PMCID: PMC215597  PMID: 6330053

Abstract

Among Tn10 insertions isolated in or near the malB region of Escherichia coli, one (zjb-729::Tn10) mapped between malK and lamB or late in malK and allowed MalT-independent expression of lamB. Tn10-dependent expression of a lamB-lacZ protein fusion was 25% of the expression of the fusion from the malK-lamB operon promoter in malTc constitutive strains. The maltoporin content of a strain carrying this Tn10 was about 20% that of a malTc malB+ strain. Transport of maltose at concentrations of below 10(-6) M was reduced about threefold. When maltoporin was present at about 50% of the level of malTc malB+ strains, maltose transport was largely restored. We conclude that maltoporin is not rate limiting for maltose transport in wild-type cells but becomes rate limiting when the ratio of maltoporin to other maltose transport components is reduced more than twofold.

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Selected References

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  1. Armstrong J. B., Adler J., Dahl M. M. Nonchemotactic mutants of Escherichia coli. J Bacteriol. 1967 Jan;93(1):390–398. doi: 10.1128/jb.93.1.390-398.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bavoil P., Hofnung M., Nikaido H. Identification of a cytoplasmic membrane-associated component of the maltose transport system of Escherichia coli. J Biol Chem. 1980 Sep 25;255(18):8366–8369. [PubMed] [Google Scholar]
  3. Bell R. M. Mutants of Escherichia coli defective in membrane phospholipid synthesis: macromolecular synthesis in an sn-glycerol 3-phosphate acyltransferase Km mutant. J Bacteriol. 1974 Mar;117(3):1065–1076. doi: 10.1128/jb.117.3.1065-1076.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Blazey D. L., Burns R. O. Transcriptional activity of the transposable element Tn10 in the Salmonella typhimurium ilvGEDA operon. Proc Natl Acad Sci U S A. 1982 Aug;79(16):5011–5015. doi: 10.1073/pnas.79.16.5011. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. 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]
  6. Boos W., Ferenci T., Shuman H. A. Formation and excretion of acetylmaltose after accumulation of maltose in Escherichia coli. J Bacteriol. 1981 May;146(2):725–732. doi: 10.1128/jb.146.2.725-732.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Brass J. M., Ehmann U., Bukau B. Reconstitution of maltose transport in Escherichia coli: conditions affecting import of maltose-binding protein into the periplasm of calcium-treated cells. J Bacteriol. 1983 Jul;155(1):97–106. doi: 10.1128/jb.155.1.97-106.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Brass J. M., Manson M. D. Reconstitution of maltose chemotaxis in Escherichia coli by addition of maltose-binding protein to calcium-treated cells of maltose regulon mutants. J Bacteriol. 1984 Mar;157(3):881–890. doi: 10.1128/jb.157.3.881-890.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Braun-Breton C., Hofnung M. Explanations accounting for transduction by bacteriophage lambda in maltose negative bacteriophage lambda resistant mutants of Escherichia coli K-12. Mol Gen Genet. 1978 Feb 16;159(2):143–149. doi: 10.1007/BF00270887. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. Ciampi M. S., Schmid M. B., Roth J. R. Transposon Tn10 provides a promoter for transcription of adjacent sequences. Proc Natl Acad Sci U S A. 1982 Aug;79(16):5016–5020. doi: 10.1073/pnas.79.16.5016. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Clement J. M., Perrin D., Hedgpeth J. Analysis of lambda receptor and beta-lactamase synthesis and export using cloned genes in a minicell system. Mol Gen Genet. 1982;185(2):302–310. doi: 10.1007/BF00330802. [DOI] [PubMed] [Google Scholar]
  13. Colonna B., Hofnung M. rho Mutations restore lamB expression in E. coli K12 strains with an inactive malB region. Mol Gen Genet. 1981;184(3):479–483. doi: 10.1007/BF00352526. [DOI] [PubMed] [Google Scholar]
  14. 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]
  15. Gilson E., Nikaido H., Hofnung M. Sequence of the malK gene in E.coli K12. Nucleic Acids Res. 1982 Nov 25;10(22):7449–7458. doi: 10.1093/nar/10.22.7449. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Hall M. N., Schwartz M., Silhavy T. J. Sequence information within the lamB genes in required for proper routing of the bacteriophage lambda receptor protein to the outer membrane of Escherichia coli K-12. J Mol Biol. 1982 Mar 25;156(1):93–112. doi: 10.1016/0022-2836(82)90461-2. [DOI] [PubMed] [Google Scholar]
  17. Hofnung M. Divergent operons and the genetic structure of the maltose B region in Escherichia coli K12. Genetics. 1974 Feb;76(2):169–184. doi: 10.1093/genetics/76.2.169. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Hofnung M., Jezierska A., Braun-Breton C. lamB mutations in E. coli K12: growth of lambda host range mutants and effect of nonsense suppressors. Mol Gen Genet. 1976 May 7;145(2):207–213. doi: 10.1007/BF00269595. [DOI] [PubMed] [Google Scholar]
  19. Hofnung M., Lepouce E., Braun-Breton C. General method for fine mapping of the Escherichia coli K-12 lamB gene: localization of missense mutations affecting bacteriophage lambda adsorption. J Bacteriol. 1981 Dec;148(3):853–860. doi: 10.1128/jb.148.3.853-860.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Kellermann O., Szmelcman S. Active transport of maltose in Escherichia coli K12. Involvement of a "periplasmic" maltose binding protein. Eur J Biochem. 1974 Aug 15;47(1):139–149. doi: 10.1111/j.1432-1033.1974.tb03677.x. [DOI] [PubMed] [Google Scholar]
  21. Kleckner N., Roth J., Botstein D. Genetic engineering in vivo using translocatable drug-resistance elements. New methods in bacterial genetics. J Mol Biol. 1977 Oct 15;116(1):125–159. doi: 10.1016/0022-2836(77)90123-1. [DOI] [PubMed] [Google Scholar]
  22. Luckey M., Nikaido H. Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli. Proc Natl Acad Sci U S A. 1980 Jan;77(1):167–171. doi: 10.1073/pnas.77.1.167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Ludtke D., Larson T. J., Beck C., Boos W. Only one gene is required for the glpT-dependent transport of sn-glycerol-3-phosphate in Escherichia coli. Mol Gen Genet. 1982;186(4):540–547. doi: 10.1007/BF00337962. [DOI] [PubMed] [Google Scholar]
  24. Pugsley A. P., Schnaitman C. A. Identification of three genes controlling production of new outer membrane pore proteins in Escherichia coli K-12. J Bacteriol. 1978 Sep;135(3):1118–1129. doi: 10.1128/jb.135.3.1118-1129.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Raibaud O., Clément J. M., Hofnung M. Structure of the malB region in Escherichia coli K12. III. Correlation of the genetic map with the restriction map. Mol Gen Genet. 1979 Jul 24;174(3):261–267. doi: 10.1007/BF00267798. [DOI] [PubMed] [Google Scholar]
  26. Randall-Hazelbauer L., Schwartz M. Isolation of the bacteriophage lambda receptor from Escherichia coli. J Bacteriol. 1973 Dec;116(3):1436–1446. doi: 10.1128/jb.116.3.1436-1446.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Schweizer H., Boos W. Transfer of the delta (argF-lac)U169 mutation between Escherichia coli strains by selection for a closely linked Tn10 insertion. Mol Gen Genet. 1983;192(1-2):293–294. doi: 10.1007/BF00327683. [DOI] [PubMed] [Google Scholar]
  28. Shuman H. A. Active transport of maltose in Escherichia coli K12. Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane. J Biol Chem. 1982 May 25;257(10):5455–5461. [PubMed] [Google Scholar]
  29. Shuman H. A. The use of gene fusions of study bacterial transport proteins. J Membr Biol. 1981;61(1):1–11. doi: 10.1007/BF01870747. [DOI] [PubMed] [Google Scholar]
  30. Silhavy T. J., Shuman H. A., Beckwith J., Schwartz M. Use of gene fusions to study outer membrane protein localization in Escherichia coli. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5411–5415. doi: 10.1073/pnas.74.12.5411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Simons R. W., Hoopes B. C., McClure W. R., Kleckner N. Three promoters near the termini of IS10: pIN, pOUT, and pIII. Cell. 1983 Sep;34(2):673–682. doi: 10.1016/0092-8674(83)90400-2. [DOI] [PubMed] [Google Scholar]
  32. Szmelcman S., Schwartz M., Silhavy T. J., Boos W. Maltose transport in Escherichia coli K12. A comparison of transport kinetics in wild-type and lambda-resistant mutants as measured by fluorescence quenching. Eur J Biochem. 1976 May 17;65(1):13–19. doi: 10.1111/j.1432-1033.1976.tb10383.x. [DOI] [PubMed] [Google Scholar]
  33. Wandersman C., Schwartz M. Mutations that alter the transport function of the LamB protein in Escherichia coli. J Bacteriol. 1982 Jul;151(1):15–21. doi: 10.1128/jb.151.1.15-21.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]

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