Skip to main content
NCBI home page
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1971 Feb 28;133(3):534–553. doi: 10.1084/jem.133.3.534

THE NATURE OF THE COLICIN K RECEPTOR OF ESCHERICHIA COLI CULLEN

Hans Ulrich Weltzien 1, Margeris A Jesaitis 1
PMCID: PMC2138940  PMID: 4939151

Abstract

Cell walls of E. coli strains B and Cullen contain specific receptors for colicin K and for the T2, T6, and C16 phages. The receptors for the bacteriocin and the T6 virus are located in the outer layers of the cell wall of these microorganisms and are absent in their cytoplasmic membrane. The receptors for colicin K, phage T2, and the T6 and C16 viruses differ in their stability toward enzymes and chemical reagents. Their specificity must therefore be determined by different chemical groupings. The colicin K receptor is inactivated by certain proteolytic enzymes and by reagents which combine with tryptophan. It is concluded therefore that proteins or peptides containing this amino acid are essential for biological activity of the receptor.

Full Text

The Full Text of this article is available as a PDF (1.1 MB).

Selected References

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

  1. ADAMS M. H. Classification of bacterial viruses: characteristics of the T5 species and of the T2, C16 species. J Bacteriol. 1952 Sep;64(3):387–396. doi: 10.1128/jb.64.3.387-396.1952. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Barman T. E., Koshland D. E., Jr A colorimetric procedure for the quantitative determination of tryptophan residues in proteins. J Biol Chem. 1967 Dec 25;242(23):5771–5776. [PubMed] [Google Scholar]
  3. Beumer J., Beumer-Jochmans M. P., Dirkx J., Dekegel D. Etat actuel des connaissances concernant la nature et la localisation des récepteurs des bactériophages dans la parol cellulaire des Shigella et des Escherichia. Bull Acad R Med Belg. 1965;5(9):749–790. [PubMed] [Google Scholar]
  4. Coyette J., Ghuysen J. M. Structure of the cell wall of Staphylococcus aureus, strain Copenhagen. IX. Teichoic acid and phage adsorption. Biochemistry. 1968 Jun;7(6):2385–2389. doi: 10.1021/bi00846a048. [DOI] [PubMed] [Google Scholar]
  5. FREDERICQ P. Action bactéricide des bactériophages des types II et III sans multiplication des corpuscules. C R Seances Soc Biol Fil. 1952 Apr;146(7-8):622–626. [PubMed] [Google Scholar]
  6. FREDERICQ P. COLICINES ET AUTRES BACTERIOCINES. Ergeb Mikrobiol Immunitatsforsch Exp Ther. 1963;37:114–161. [PubMed] [Google Scholar]
  7. FREDERICQ P. Colicines et bactériophages. Ann Inst Pasteur (Paris) 1953 Jan;84(1):294–312. [PubMed] [Google Scholar]
  8. FREDERICQ P. Résistance et immunité aux colicines. C R Seances Soc Biol Fil. 1956;150(7):1514–1517. [PubMed] [Google Scholar]
  9. GEOBEL W. F., JESAITIS M. A. The somatic antigen of a phage-resistant variant of Phase II Shigella sonnei. J Exp Med. 1952 Nov;96(5):425–438. doi: 10.1084/jem.96.5.425. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. GOEBEL W. F., BARRY G. T., SHEDLOVSKY T. Colicine K. I. The production of colicine K in media maintained at constant pH. J Exp Med. 1956 May 1;103(5):577–588. doi: 10.1084/jem.103.5.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. GOEBEL W. F., PERLMANN G. E. The effect of lithium periodate on crystalline bovine serum albumin. J Exp Med. 1949 May;89(5):479–489. doi: 10.1084/jem.89.5.479. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Guterman S. K., Luria S. E. Escherichia coli: strains that excrete an inhibitor of colicin B. Science. 1969 Jun 20;164(3886):1414–1414. doi: 10.1126/science.164.3886.1414. [DOI] [PubMed] [Google Scholar]
  13. JESAITIS M. A., GOEBEL W. F. The chemical and antiviral properties of the somatic antigen of Phase II Shigella sonnei. J Exp Med. 1952 Nov;96(5):409–424. doi: 10.1084/jem.96.5.409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Jesaitis M. A. The nature of colicin K from Proteus mirabilis. J Exp Med. 1970 May 1;131(5):1016–1038. doi: 10.1084/jem.131.5.1016. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. KRAUSE R. M. Studies on bacteriophages of hemolytic streptococci. I. Factors influencing the interaction of phage and susceptible host cell. J Exp Med. 1957 Sep 1;106(3):365–384. doi: 10.1084/jem.106.3.365. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. MAYR-HARTING A. THE ADSORPTION OF COLICINE. J Pathol Bacteriol. 1964 Apr;87:255–266. doi: 10.1002/path.1700870206. [DOI] [PubMed] [Google Scholar]
  17. MILLER E. M., GOEBEL W. F. Studies on bacteriophage; the relationship between the somatic antigens of Shigella sonnei and their susceptibilitv to bacterial viruses. J Exp Med. 1949 Sep;90(3):255–265. doi: 10.1084/jem.90.3.255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. MORSE S. I. Studies on the interactions between components of Staphylococcus aureus and Staphylococcus bacteriophage. J Exp Med. 1962 Aug 1;116:247–251. doi: 10.1084/jem.116.2.247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Maeda A., Nomura M. Interaction of colicins with bacterial cells. I. Studies with radioactive colicins. J Bacteriol. 1966 Feb;91(2):685–694. doi: 10.1128/jb.91.2.685-694.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Marotel-Schirmann J., Barbu E. Quelques données sur les récepteurs des colicines. C R Acad Sci Hebd Seances Acad Sci D. 1969 Aug 25;269(8):866–869. [PubMed] [Google Scholar]
  21. Miura T., Mizushima S. Separation and properties of outer and cytoplasmic membranes in Escherichia coli. Biochim Biophys Acta. 1969;193(2):268–276. doi: 10.1016/0005-2736(69)90188-6. [DOI] [PubMed] [Google Scholar]
  22. Miura T., Mizushima S. Separation by density gradient centrifugation of two types of membranes from spheroplast membrane of Escherichia coli K12. Biochim Biophys Acta. 1968 Jan 3;150(1):159–161. doi: 10.1016/0005-2736(68)90020-5. [DOI] [PubMed] [Google Scholar]
  23. NOMURA M., NAKAMURA M. Reversibility of inhibition of nucleic acids and protein synthesis by colicin K. Biochem Biophys Res Commun. 1962 May 4;7:306–309. doi: 10.1016/0006-291x(62)90196-1. [DOI] [PubMed] [Google Scholar]
  24. Nagel de Zwaig R., Luria S. E. Genetics and physiology of colicin-tolerant mutants of Escherichia coli. J Bacteriol. 1967 Oct;94(4):1112–1123. doi: 10.1128/jb.94.4.1112-1123.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Nomura M., Witten C. Interaction of colicins with bacterial cells. 3. Colicin-tolerant mutations in Escherichia coli. J Bacteriol. 1967 Oct;94(4):1093–1111. doi: 10.1128/jb.94.4.1093-1111.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. OROSZLAN S. I., MORA P. T. DISSOCIATION AND RECONSTITUTION OF AN ENDOTOXIN. Biochem Biophys Res Commun. 1963 Aug 14;12:345–349. doi: 10.1016/0006-291x(63)90102-5. [DOI] [PubMed] [Google Scholar]
  27. Ribi E., Anacker R. L., Brown R., Haskins W. T., Malmgren B., Milner K. C., Rudbach J. A. Reaction of endotoxin and surfactants. I. Physical and biological properties of endotoxin treated with sodium deoxycholate. J Bacteriol. 1966 Nov;92(5):1493–1509. doi: 10.1128/jb.92.5.1493-1509.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Riordan J. F., Sokolovsky M., Vallee B. L. The functional tyrosyl residues of carboxypeptidase A. Nitration with tetranitromethane. Biochemistry. 1967 Nov;6(11):3609–3617. doi: 10.1021/bi00863a036. [DOI] [PubMed] [Google Scholar]
  29. Scoffone E., Fontana A., Rocchi R. Sulfenyl halides as modifying reagents for polypeptides and proteins. I. Modification of tryptophan residues. Biochemistry. 1968 Mar;7(3):971–979. doi: 10.1021/bi00843a014. [DOI] [PubMed] [Google Scholar]
  30. Shapiro A. L., Viñuela E., Maizel J. V., Jr Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem Biophys Res Commun. 1967 Sep 7;28(5):815–820. doi: 10.1016/0006-291x(67)90391-9. [DOI] [PubMed] [Google Scholar]
  31. Smarda J., Schuhmann E. Do certain colicines and phages share common receptors? Nature. 1967 Feb 11;213(5076):614–614. doi: 10.1038/213614a0. [DOI] [PubMed] [Google Scholar]
  32. Tsao S. S., Goebel W. F. Colicin K. 8. The immunological properties of mitomycin-induced colicin K. J Exp Med. 1969 Dec 1;130(6):1313–1335. doi: 10.1084/jem.130.6.1313. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Vallee B. L., Riordan J. F. Chemical approaches to the properties of active sites of enzymes. Annu Rev Biochem. 1969;38:733–794. doi: 10.1146/annurev.bi.38.070169.003505. [DOI] [PubMed] [Google Scholar]
  34. Vidaver A. K., Brock T. D. Purification and properties of a bacteriophage receptor material from Streptococcus faecium. Biochim Biophys Acta. 1966 Jun 29;121(2):298–314. doi: 10.1016/0304-4165(66)90119-x. [DOI] [PubMed] [Google Scholar]
  35. WEIDEL W., FRANK H., MARTIN H. H. The rigid layer of the cell wall of Escherichia coli strain B. J Gen Microbiol. 1960 Feb;22:158–166. doi: 10.1099/00221287-22-1-158. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES