Molecular and General Genetics MGG

, Volume 199, Issue 1, pp 111–116 | Cite as

Regulation of haemolysin synthesis in E. coli determined by HLY genes of human origin

  • J.-M. Nicaud
  • N. Mackman
  • L. Gray
  • I. B. Holland


We have previously reported the secretion of a 107K polypeptide into the medium from a haemolytic E. coli K12 strain (Mackman and Holland 1984a). In addition, we demonstrated that haemolysin production was correlated with the presence of this polypeptide in the growth medium in a large number of E. coli isolates of human and animal origin (Mackman and Holland 1984b).

In this paper we confirm that the 107K polypeptide is indeed haemolysin: both haemolytic activity and the 107K polypeptide show a similar pattern of accumulation during the growth cycle; identical levels are produced in three different growth media; they have the same half-life in minimal medium. The results also show that the expression of haemolysin is not influenced by the growth medium or subject to catabolite repression. However, expression is apparently switched off as cells enter the late exponential phase of growth. Finally, we present data indicating that the previously reported variation in haemolysin production in different media is entirely due to the instability of the haemoolysin itself. Degradation of the 107K polypeptide in the medium was accompanied by the accumulation of a major breakdown product of 60K.


Polypeptide Growth Medium Minimal Medium Exponential Phase Growth Cycle 
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  1. Ames GF (1974) Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs. J Biol Chem 249:639–644Google Scholar
  2. Boyd A, Holland IB (1979) Regulation of the synthesis of surface protein in the cell cycle of E. coli B/r. Cell 18:287–296Google Scholar
  3. Casadaban MJ, Chou J, Cohen S (1980) In vitro gene fusions that join an enzymatically active β-galactosidase segment to amino-terminal fragments of exogenous proteins. Escherichia coli plasmid vectors for the detection and cloning of translational initiation signals. J Bacteriol 143:970–980Google Scholar
  4. Goebel W, Hedgpeth J (1982) Cloning and functional characterization of the plasmid-encoded hemolysin determinant of Escherichia coli. J Bacteriol 151:1290–1298Google Scholar
  5. Hacker J, Knapp S, Goebel W (1983) Spontaneous deletions and flanking regions of the chromosomally inherited hemolysin determinant of an Escherichia coli 06 strain. J Bacteriol 154:1145–1152Google Scholar
  6. Härtlein M, Schießl S, Wagner W, Rdest V, Kreft J, Goebel W (1983) Transport of haemolysin by Escherichia coli. J Cell Biochem 22:87–97Google Scholar
  7. Jorgensen S, Short E, Kurtz H, Mussen H, Wu G (1976) Origins of α-haemolysin produced by E. coli. J Med Microbiol 9:173–189Google Scholar
  8. Juarez A, Goebel W (1984) Chromosomal mutation that affects excretion of hemolysin in Escherichia coli. J Bacteriol 159:1083–1085Google Scholar
  9. Mackman N, Holland IB (1984a) Secretion of a 107K dalton polypeptide into the medium from a haemolytic E. coli K12 strain. Mol Gen Genet 193:312–315Google Scholar
  10. Mackman N, Holland IB (1984b) Functional characterization of a cloned information for the secretion of a 107K polypeptide. Mol Gen Genet 196:129–134Google Scholar
  11. Miller JH (1972) Experiments. In: Molecular genetics, Cold Spring Harbor Laboratory, New YorkGoogle Scholar
  12. Müller D, Hughes C, Goebel W (1983) Relationship between plasmid and chromosomal hemolysin determinants of Escherichia coli. J Bacteriol 153:846–851Google Scholar
  13. Noegel A, Rdest U, Springer W, Goebel W (1979) Plasmid cistrons controlling synthesis and excretion of the exotoxin α Haemolysin of Escherichia coli. Mol Gen Genet 175:343–350Google Scholar
  14. Pollock MR (1962) Exoenzymes. In: Gunsolus IC, Stanier RY (eds) The bacteria. New York, 4, pp 121–178Google Scholar
  15. Pugsley AP (1984) The ins and outs of colicins. Part I: Production and translocation across membranes. Microbiol Sci 1:168–174Google Scholar
  16. Raynaud M, Alouf JE (1970) Intracellular versus extracellular toxins. In: Ajl SJ, Kadis S, Montie TC (eds) Microbiol toxins. New York, 1, p 67Google Scholar
  17. Snyder IS, Koch NA (1966) Production and characteristics of haemolysins of Escherichia coli. J Bacteriol 91:763–767Google Scholar
  18. Springer W, Goebel W (1980) Synthesis and secretion of hemolysin by Escherichia coli. J Bacteriol 144:53–59Google Scholar
  19. Stark J, Shuster C (1983) The structure of cloned hemolysin DNA from plasmid pHly185. Plasmid 10:45–54Google Scholar
  20. Welch R, Hall R, Falkow S (1983) Molecular cloning and physical characterization of a chromosomal hemolysin from Escherichia coli. Infect Immun 42:178–186Google Scholar
  21. Zabala JC, Garcia-Lobo JM, Diaz-Aroca E, de la Cruz F, Ortiz JM (1984) Escherichia coli alpha-haemolysin synthesis and export genes are flanked by a direct repetition of IS91-like elements. Mol Gen Genet 197:90–97Google Scholar

Copyright information

© Springer-Verlag 1985

Authors and Affiliations

  • J.-M. Nicaud
    • 1
  • N. Mackman
    • 1
  • L. Gray
    • 1
  • I. B. Holland
    • 1
  1. 1.Department of GeneticsUniversity of LeicesterLeicesterUnited Kingdom

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