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Gene Review

hlyE  -  hemolysin E

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1170, JW5181, clyA, hpr, sheA, ...
 
 
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Disease relevance of hlyE

 

High impact information on hlyE

  • Identification and characterization of an amphipathic leucine zipper-like motif in Escherichia coli toxin hemolysin E. Plausible role in the assembly and membrane destabilization [3].
  • The results presented here indicate that this H-205 (amino acid 205-234) segment may be an important structural element in hemolysin E, which could play a significant role in the binding and assembly of the toxin in the target cell membrane and its destabilization [3].
  • The novel pore-forming toxin hemolysin E (HlyE, ClyA, or SheA) consists of a long four-helix bundle with a subdomain (beta tongue) that interacts with target membranes at one pole and an additional helix (alpha(G)) that, with the four long helices, forms a five-helix bundle (tail domain) at the other pole [4].
  • Here in vivo transcription studies reveal that FNR occupies the hlyE promoter more frequently than CRP, providing a mechanism for the moderate upregulation of hlyE expression in response to two distinct environmental signals (oxygen and glucose starvation) [5].
  • Finally, the identification of a SlyA binding site that overlaps the H-NS I site in PhlyE suggests a mechanism to explain how SlyA overproduction enhances hlyE expression by antagonizing the negative effects of H-NS [5].
 

Chemical compound and disease context of hlyE

  • Here it is shown that the JM4660 hlyE sequence encodes Gly, not Arg, at position 188 and that substitution of Gly188 by Arg in E. coli K-12 HlyE abolishes activity, emphasizing the importance of the head domain in HlyE function [6].
 

Biological context of hlyE

  • TnphoA mutagenesis of hlyE shows that secretion from the cytoplasm to the periplasm does not require the carboxyl-terminal region of HlyE [6].
 

Associations of hlyE with chemical compounds

  • In order to evaluate the possible structural and functional roles of this segment in HlyE, a 30-residue peptide (H-205) corresponding to the leucine zipper motif (amino acid 205-234) and two mutant peptides of the same size were synthesized and labeled by fluorescent probes at their N termini [3].
 

Analytical, diagnostic and therapeutic context of hlyE

References

  1. Altering the anaerobic transcription factor FNR confers a hemolytic phenotype on Escherichia coli K12. Ralph, E.T., Guest, J.R., Green, J. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  2. E. coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy. Wallace, A.J., Stillman, T.J., Atkins, A., Jamieson, S.J., Bullough, P.A., Green, J., Artymiuk, P.J. Cell (2000) [Pubmed]
  3. Identification and characterization of an amphipathic leucine zipper-like motif in Escherichia coli toxin hemolysin E. Plausible role in the assembly and membrane destabilization. Yadav, S.P., Kundu, B., Ghosh, J.K. J. Biol. Chem. (2003) [Pubmed]
  4. Structure-function relationships of a novel bacterial toxin, hemolysin E. The role of alpha G. Atkins, A., Wyborn, N.R., Wallace, A.J., Stillman, T.J., Black, L.K., Fielding, A.B., Hisakado, M., Artymiuk, P.J., Green, J. J. Biol. Chem. (2000) [Pubmed]
  5. Regulation of Escherichia coli hemolysin E expression by H-NS and Salmonella SlyA. Wyborn, N.R., Stapleton, M.R., Norte, V.A., Roberts, R.E., Grafton, J., Green, J. J. Bacteriol. (2004) [Pubmed]
  6. Properties of haemolysin E (HlyE) from a pathogenic Escherichia coli avian isolate and studies of HlyE export. Wyborn, N.R., Clark, A., Roberts, R.E., Jamieson, S.J., Tzokov, S., Bullough, P.A., Stillman, T.J., Artymiuk, P.J., Galen, J.E., Zhao, L., Levine, M.M., Green, J. Microbiology (Reading, Engl.) (2004) [Pubmed]
 
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