Translocation and Compartmentalization of Escherichia Coli Hemolysin (HlyA)

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1990 Jul 1

PMID 2193915

Citations 12

Authors

W Speth

B Imhof

I Gentschev

W Goebel

Affiliations

Soon will be listed here.

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.

Citing Articles

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