Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1975 Oct;124(1):119–126. doi: 10.1128/jb.124.1.119-126.1975

Role of the receptor for bacteriophage lambda in the functioning of the maltose chemoreceptor of Escherichia coli.

G L Hazelbauer
PMCID: PMC235872  PMID: 1100597

Abstract

Chemotaxis towards maltose is specifically defective in many strains of Escherichia coli carrying mutations affecting lamB, the gene coding for the outer membrane receptor for bacteriophage lambda. However, with one exception, the most extreme effect of lamB mutants on the maltose response as determined in the capillary assay is a shift to higher sugar concentrations and a reduction in the number of bacteria accumulated to about 25% of the wild-type level. The severity of the taxis defect is strongly correlated with reduced ability of the cells to take up the maltose present at 1 and 10 muM. Evidence presented here and in the accompanying paper indicates that the lambda receptor is involved in the transport of maltose at these concentrations. The effects of lamB mutations on maltose taxis can be explained by postulating that the high-affinity maltose transport system in which the lambda receptor participates transfers maltose from the surrounding medium across the outer membrane and into the periplasmic space. If the maltose chemoreceptor detects sugar present in the periplasmic space, and not molecules external to the outer membrane, then defective transport of low concentrations of maltose into the periplasm would result in the observed apparent reduction in the sensitivity of the maltose receptor. Thus, the lambda receptor protein would participate in maltose chemorecepton only indirectly through its role in maltose transport.

Full text

PDF
125

Selected References

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

  1. Adler J. A method for measuring chemotaxis and use of the method to determine optimum conditions for chemotaxis by Escherichia coli. J Gen Microbiol. 1973 Jan;74(1):77–91. doi: 10.1099/00221287-74-1-77. [DOI] [PubMed] [Google Scholar]
  2. Adler J. Chemoreceptors in bacteria. Science. 1969 Dec 26;166(3913):1588–1597. doi: 10.1126/science.166.3913.1588. [DOI] [PubMed] [Google Scholar]
  3. Adler J. Chemotaxis in bacteria. Science. 1966 Aug 12;153(3737):708–716. doi: 10.1126/science.153.3737.708. [DOI] [PubMed] [Google Scholar]
  4. Adler J. Chemotaxis in bacteria. Annu Rev Biochem. 1975;44:341–356. doi: 10.1146/annurev.bi.44.070175.002013. [DOI] [PubMed] [Google Scholar]
  5. Boos W. The galactose binding protein and its relationship to the beta-methylgalactoside permease from Escherichia coli. Eur J Biochem. 1969 Aug;10(1):66–73. doi: 10.1111/j.1432-1033.1969.tb00656.x. [DOI] [PubMed] [Google Scholar]
  6. Di Masi D. R., White J. C., Schnaitman C. A., Bradbeer C. Transport of vitamin B12 in Escherichia coli: common receptor sites for vitamin B12 and the E colicins on the outer membrane of the cell envelope. J Bacteriol. 1973 Aug;115(2):506–513. doi: 10.1128/jb.115.2.506-513.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Futrelle R. P., Berg H. C. Specification of gradients used for studies of chemotaxis. Nature. 1972 Oct 27;239(5374):517–518. doi: 10.1038/239517a0. [DOI] [PubMed] [Google Scholar]
  8. Gustafsson P., Nordström K., Normark S. Outer penetration barrier of Escherichia coli K-12: kinetics of the uptake of gentian violet by wild type and envelope mutants. J Bacteriol. 1973 Nov;116(2):893–900. doi: 10.1128/jb.116.2.893-900.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hazelbauer G. L., Adler J. Role of the galactose binding protein in chemotaxis of Escherichia coli toward galactose. Nat New Biol. 1971 Mar 24;230(12):101–104. doi: 10.1038/newbio230101a0. [DOI] [PubMed] [Google Scholar]
  10. Hazelbauer G. L. Maltose chemoreceptor of Escherichia coli. J Bacteriol. 1975 Apr;122(1):206–214. doi: 10.1128/jb.122.1.206-214.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. 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]
  12. Hofnung M., Hatfield D., Schwartz M. malB region in Escherichia coli K-12: characterization of new mutations. J Bacteriol. 1974 Jan;117(1):40–47. doi: 10.1128/jb.117.1.40-47.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. LEIVE L. A NONSPECIFIC INCREASE IN PERMEABILITY IN ESCHERICHIA COLI PRODUCED BY EDTA. Proc Natl Acad Sci U S A. 1965 Apr;53:745–750. doi: 10.1073/pnas.53.4.745. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Lofgren K. W., Fox C. F. Attractant-directed motility in Escherichia coli: requirement for a fluid lipid phase. J Bacteriol. 1974 Jun;118(3):1181–1182. doi: 10.1128/jb.118.3.1181-1182.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Mesibov R., Ordal G. W., Adler J. The range of attractant concentrations for bacterial chemotaxis and the threshold and size of response over this range. Weber law and related phenomena. J Gen Physiol. 1973 Aug;62(2):203–223. doi: 10.1085/jgp.62.2.203. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Ordal G. W., Adler J. Isolation and complementation of mutants in galactose taxis and transport. J Bacteriol. 1974 Feb;117(2):509–516. doi: 10.1128/jb.117.2.509-516.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Ordal G. W., Adler J. Properties of mutants in galactose taxis and transport. J Bacteriol. 1974 Feb;117(2):517–526. doi: 10.1128/jb.117.2.517-526.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. 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]
  20. Silhavy T. J., Szmelcman S., Boos W., Schwartz M. On the significance of the retention of ligand by protein. Proc Natl Acad Sci U S A. 1975 Jun;72(6):2120–2124. doi: 10.1073/pnas.72.6.2120. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Szmelcman S., Hofnung M. Maltose transport in Escherichia coli K-12: involvement of the bacteriophage lambda receptor. J Bacteriol. 1975 Oct;124(1):112–118. doi: 10.1128/jb.124.1.112-118.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Tamaki S., Sato T., Matsuhashi M. Role of lipopolysaccharides in antibiotic resistance and bacteriophage adsorption of Escherichia coli K-12. J Bacteriol. 1971 Mar;105(3):968–975. doi: 10.1128/jb.105.3.968-975.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES