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. 1979 Apr;138(1):33–39. doi: 10.1128/jb.138.1.33-39.1979

Receptor for bacteriophage lambda of Escherichia coli forms larger pores in black lipid membranes than the matrix protein (porin).

B A Boehler-Kohler, W Boos, R Dieterle, R Benz
PMCID: PMC218234  PMID: 374375

Abstract

The receptor for phage lambda in Escherichia coli was isolated by cholate extraction and purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Protein bands corresponding to the monomer and the dimer were eluted from the gel and tested for their activity to inactivate phage lambda and to form pores in black lipid membranes. It was found that only the dimer inactivated phage lambda, whereas both the monomer and the dimer were active in forming pores. The pore characteristics were similar to those exhibited by the matrix protein (porin) (R. Benz, K. Janko, W. Boos, and P. Läuger, Biochim. Biophys. Acta 511:305--319, 1978). In comparison, the lambda receptor showed a somewhat higher degree of cation specificity, and its pore size was larger. Assuming that the thickness of the outer membrane is 7.5 nm and that the pore is an ideal hydrophilic channel, the pore diameter in vivo was estimated to be 1.6 nm for the lambda receptor and 1.2 nm for the matrix protein.

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Selected References

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  1. Bangham J. A., Lea E. J. The interaction of detergents with bilayer lipid membranes. Biochim Biophys Acta. 1978 Aug 17;511(3):388–396. doi: 10.1016/0005-2736(78)90275-4. [DOI] [PubMed] [Google Scholar]
  2. Bavoil P., Nikaido H., von Meyenburg K. Pleiotropic transport mutants of Escherichia coli lack porin, a major outer membrane protein. Mol Gen Genet. 1977 Dec 14;158(1):23–33. doi: 10.1007/BF00455116. [DOI] [PubMed] [Google Scholar]
  3. Benz R., Boehler-Kohler B. A., Dieterle R., Boos W. Porin activity in the osmotic shock fluid of Escherichia coli. J Bacteriol. 1978 Sep;135(3):1080–1090. doi: 10.1128/jb.135.3.1080-1090.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Benz R., Janko K., Boos W., Läuger P. Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta. 1978 Aug 17;511(3):305–319. doi: 10.1016/0005-2736(78)90269-9. [DOI] [PubMed] [Google Scholar]
  5. Benz R., Janko K., Läuger P. Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta. 1979 Mar 8;551(2):238–247. doi: 10.1016/0005-2736(89)90002-3. [DOI] [PubMed] [Google Scholar]
  6. Benz R., Stark G., Janko K., Läuger P. Valinomycin-mediated ion transport through neutral lipid membranes: influence of hydrocarbon chain length and temperature. J Membr Biol. 1973;14(4):339–364. doi: 10.1007/BF01868084. [DOI] [PubMed] [Google Scholar]
  7. Braun V., Krieger-Brauer H. J. Interrelationship of the phage lambda receptor protein and maltose transport in mutants of Escherichia coli K12. Biochim Biophys Acta. 1977 Aug 15;469(1):89–98. doi: 10.1016/0005-2736(77)90328-5. [DOI] [PubMed] [Google Scholar]
  8. DiRienzo J. M., Nakamura K., Inouye M. The outer membrane proteins of Gram-negative bacteria: biosynthesis, assembly, and functions. Annu Rev Biochem. 1978;47:481–532. doi: 10.1146/annurev.bi.47.070178.002405. [DOI] [PubMed] [Google Scholar]
  9. Edermann R., Hindennach I., Henning U. Major proteins of the Escherichia coli outer cell envelope membrane. Preliminary characterization of the phage lambda receptor protein. FEBS Lett. 1978 Apr 1;88(1):71–74. doi: 10.1016/0014-5793(78)80609-7. [DOI] [PubMed] [Google Scholar]
  10. Hindennach I., Henning U. The major proteins of the Excherichia coli outer cell envelope membrane. Preparative isolation of all major membrane proteins. Eur J Biochem. 1975 Nov 1;59(1):207–213. doi: 10.1111/j.1432-1033.1975.tb02443.x. [DOI] [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. 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]
  13. Lin E. C. The genetics of bacterial transport systems. Annu Rev Genet. 1970;4:225–262. doi: 10.1146/annurev.ge.04.120170.001301. [DOI] [PubMed] [Google Scholar]
  14. Nakae T. Identification of the outer membrane protein of E. coli that produces transmembrane channels in reconstituted vesicle membranes. Biochem Biophys Res Commun. 1976 Aug 9;71(3):877–884. doi: 10.1016/0006-291x(76)90913-x. [DOI] [PubMed] [Google Scholar]
  15. Nakae T. Outer membrane of Salmonella typhimurium: reconstitution of sucrose-permeable membrane vesicles. Biochem Biophys Res Commun. 1975 Jun 16;64(4):1224–1230. doi: 10.1016/0006-291x(75)90823-2. [DOI] [PubMed] [Google Scholar]
  16. Nakae T. Outer membrane of Salmonella. Isolation of protein complex that produces transmembrane channels. J Biol Chem. 1976 Apr 10;251(7):2176–2178. [PubMed] [Google Scholar]
  17. Neu H. C., Heppel L. A. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J Biol Chem. 1965 Sep;240(9):3685–3692. [PubMed] [Google Scholar]
  18. 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]
  19. Rosenbusch J. P. Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding. J Biol Chem. 1974 Dec 25;249(24):8019–8029. [PubMed] [Google Scholar]
  20. Schaffner W., Weissmann C. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal Biochem. 1973 Dec;56(2):502–514. doi: 10.1016/0003-2697(73)90217-0. [DOI] [PubMed] [Google Scholar]
  21. Schwartz M. Sur l'existence chez Escherichia coli K 12 d'une régulation commune à la biosynthèse des récepteurs du bactériophage et au métabolisme du maltose. Ann Inst Pasteur (Paris) 1967 Nov;113(5):685–704. [PubMed] [Google Scholar]
  22. Studier F. W. Analysis of bacteriophage T7 early RNAs and proteins on slab gels. J Mol Biol. 1973 Sep 15;79(2):237–248. doi: 10.1016/0022-2836(73)90003-x. [DOI] [PubMed] [Google Scholar]
  23. 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]
  24. 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]
  25. WIESMEYER H., COHN M. The characterization of the pathway of maltose utilization by Escherichia coli. III. Adescription of the concentrating mechanism. Biochim Biophys Acta. 1960 Apr 22;39:440–447. doi: 10.1016/0006-3002(60)90196-7. [DOI] [PubMed] [Google Scholar]
  26. von Meyenburg Kaspar Transport-limited growth rates in a mutant of Escherichia coli. J Bacteriol. 1971 Sep;107(3):878–888. doi: 10.1128/jb.107.3.878-888.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. von Meyenburg K., Nikaido H. Outer membrane of gram-negative bacteria. XVII. Secificity of transport process catalyzed by the lambda-receptor protein in Escherichia coli. Biochem Biophys Res Commun. 1977 Oct 10;78(3):1100–1107. doi: 10.1016/0006-291x(77)90534-4. [DOI] [PubMed] [Google Scholar]

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