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. 1990 Jul;172(7):3711–3717. doi: 10.1128/jb.172.7.3711-3717.1990

Translocation and compartmentalization of Escherichia coli hemolysin (HlyA).

R L Oropeza-Wekerle 1, W Speth 1, B Imhof 1, I Gentschev 1, W Goebel 1
PMCID: PMC213348  PMID: 2193915

Abstract

Hemolysin plasmids were constructed with mutations in hlyB, hlyD, or both transport genes. The localization of hemolysin activity and HlyA protein in these mutants was analyzed by biochemical and immunological methods. It was found that mutants defective in hlyB accumulated internal hemolysin, part of which was associated with the inner membrane and was degraded in the late logarithmic growth phase. In an HlyB+ HlyD- mutant, hemolysin was predominantly localized in the membrane compartment. Labeling of these Escherichia coli cells with anti-HlyA antibody indicated that part of HlyA, presumably the C-terminal end but not the pore-forming domains, was already transported to the cellular surface. This finding suggests that HlyB is able to recognize the C-terminal signal of the HlyA protein and to initiate its translocation across the membranes.

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Selected References

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

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