Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1975 Jul;123(1):96–101. doi: 10.1128/jb.123.1.96-101.1975

Genetics of resistance to colicins in Escherichia coli K-12: cross-resistance among colicins of group B.

J K Davies, P Reeves
PMCID: PMC235695  PMID: 124727

Abstract

This paper describes the isolation of mutants resistant to colicins of group B (i.e., colicins B, D, G, H, Ia, Ib, M, Q, S1, and V). The 145 mutants studied in detail can be divided into nine phentopyic classes, based on their colicin-resistance patterns. They include the previously isolated tonA, tonB exbB and cir mutants. Each of the different phenotypic classes of mutants has been partially characterized, and some approximately mapped. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis has revealed substantial changes in the composition of the outer membrane proteins of exbB and tonB mutants.

Full text

PDF
96

Selected References

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

  1. Braun V., Schaller K., Wolff H. A common receptor protein for phage T5 and colicin M in the outer membrane of Escherichia coli B. Biochim Biophys Acta. 1973 Sep 27;323(1):87–97. doi: 10.1016/0005-2736(73)90433-1. [DOI] [PubMed] [Google Scholar]
  2. Braun V., Wolff H. Characterization of the receptor protein for phage T5 and colicin M in the outer membrane of E. coli B. FEBS Lett. 1973 Aug 1;34(1):77–80. doi: 10.1016/0014-5793(73)80707-0. [DOI] [PubMed] [Google Scholar]
  3. CURTIS S. R., 3rd CHROMOSOMAL ABERRATIONS ASSOCIATED WITH MUTATIONS TO BACTERIOPHAGE RESISTANCE IN ESCHERICHIA COLI. J Bacteriol. 1965 Jan;89:28–40. doi: 10.1128/jb.89.1.28-40.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cardelli J., Konisky J. Isolation and characterization of an Escherichia coli mutant tolerant to colicins Ia and Ib. J Bacteriol. 1974 Aug;119(2):379–385. doi: 10.1128/jb.119.2.379-385.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Davies J. K., Reeves P. Genetics of resistance to colicins in Escherichia coli K-12: cross-resistance among colicins of group A. J Bacteriol. 1975 Jul;123(1):102–117. doi: 10.1128/jb.123.1.102-117.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. FREDERICQ P. Origine spontanée des mutants de E. coli V produisant la colicine M. Antonie Van Leeuwenhoek. 1951;17(4):227–231. doi: 10.1007/BF02062267. [DOI] [PubMed] [Google Scholar]
  7. FREDERICQ P. Recherches sur les caractères et la distribution des souches productrices de diverses colicines dans les selles normales et pathologiques. Bull Acad R Med Belg. 1953 Feb;18(2):126–139. [PubMed] [Google Scholar]
  8. Fredericq P., Smarda J. Complexité du facteur colicinogène B. Ann Inst Pasteur (Paris) 1970 Jun;118(6):767–774. [PubMed] [Google Scholar]
  9. GRATIA J. P. R'ESISTANCE 'A LA COLICINE B CHEZ E. COLI. RELATIONS DE SP'ECIFICIT'E ENTRE COLICINES B, I ET V ET PHAGE T-4. ETUDE G'EN'ETIQUE. Ann Inst Pasteur (Paris) 1964 Nov;107:SUPPL–SUPPL:151. [PubMed] [Google Scholar]
  10. Guterman S. K. Colicin B: mode of action and inhibition by enterochelin. J Bacteriol. 1973 Jun;114(3):1217–1224. doi: 10.1128/jb.114.3.1217-1224.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Guterman S. K., Dann L. Excretion of enterochelin by exbA and exbB mutants of Escherichia coli. J Bacteriol. 1973 Jun;114(3):1225–1230. doi: 10.1128/jb.114.3.1225-1230.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Guterman S. K. Inhibition of colicin B by enterochelin. Biochem Biophys Res Commun. 1971 Sep;44(5):1149–1155. doi: 10.1016/s0006-291x(71)80206-1. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. Neville D. M., Jr Molecular weight determination of protein-dodecyl sulfate complexes by gel electrophoresis in a discontinuous buffer system. J Biol Chem. 1971 Oct 25;246(20):6328–6334. [PubMed] [Google Scholar]
  15. Schacterle G. R., Pollack R. L. A simplified method for the quantitative assay of small amounts of protein in biologic material. Anal Biochem. 1973 Feb;51(2):654–655. doi: 10.1016/0003-2697(73)90523-x. [DOI] [PubMed] [Google Scholar]
  16. Schnaitman C. A. Outer membrane proteins of Escherichia coli. I. Effect of preparative conditions on the migration of protein in polyacrylamide gels. Arch Biochem Biophys. 1973 Aug;157(2):541–552. doi: 10.1016/0003-9861(73)90673-5. [DOI] [PubMed] [Google Scholar]
  17. Schnaitman C. A. Solubilization of the cytoplasmic membrane of Escherichia coli by Triton X-100. J Bacteriol. 1971 Oct;108(1):545–552. doi: 10.1128/jb.108.1.545-552.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Swank R. T., Munkres K. D. Molecular weight analysis of oligopeptides by electrophoresis in polyacrylamide gel with sodium dodecyl sulfate. Anal Biochem. 1971 Feb;39(2):462–477. doi: 10.1016/0003-2697(71)90436-2. [DOI] [PubMed] [Google Scholar]
  19. Taylor A. L., Trotter C. D. Linkage map of Escherichia coli strain K-12. Bacteriol Rev. 1972 Dec;36(4):504–524. doi: 10.1128/br.36.4.504-524.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Timmis K. Purification and characterization of colicin D. J Bacteriol. 1972 Jan;109(1):12–20. doi: 10.1128/jb.109.1.12-20.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES