Cellular localization and export of the soluble haemolysin of Vibrio cholerae El Tor.
The cellular location of the haemolysin of Vibrio cholerae El Tor strain 017 has been analyzed. This protein is found both in the periplasmic space and the extracellular medium in Vibrio cholerae. However, when the cloned gene, present on plasmid pPM431, is introduced into E. coli K-12 this protein remains localized predominantly in the periplasmic space with no activity detected in the extracellular medium. Mutants of E. coli K-12 (tolA and tolB) which leak periplasmic proteins mimic excretion and release the haemolysin into the growth medium. Secretion of haemolysin into the periplasm is independent of perA (envZ) and in fact, mutants in perA (envZ) harbouring pPM431 show hyperproduction of periplasmic haemolysin. These results in conjunction with those for other V. cholerae extracellular proteins suggest that although E. coli K-12 can secrete these proteins into the periplasm, it lacks a specific excretion mechanism, present in V. cholerae, for the release of soluble proteins into the growth medium.
D000818:Animals; D002458:Cell Fractionation; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D005796:Genes; D005798:Genes, Bacterial; D006460:Hemolysin Proteins / Q000235:genetics* / Q000302:isolation & purification; D006461:Hemolysis; D010957:Plasmids; D012756:Sheep; D013045:Species Specificity; D013347:Subcellular Fractions / Q000032:analysis; D014169:Transformation, Bacterial; D014734:Vibrio cholerae / Q000235:genetics*
D006460:Hemolysin Proteins