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Article

Identification of individual amino acids required for secretion within the haemolysin (HlyA) C-terminal targeting region.

Molecular microbiology - 1 Jun 1992

Kenny B, Taylor S, Holland I B

Abstract excerpt

The release of haemolysin from Escherichia coli involves direct secretion across both the inner and outer membranes. Secretion of HlyA is dependent upon a specific membrane export complex composed of HlyB, -D and possibly TolC. HlyA is targeted to the medium via the membrane translocation complex, by a novel C-terminal secretion signal. Previous studies involving deletion and fusion analyses have given...

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Identifiers

PMID: 1625577
DOI: 10.1111/j.1365-2958.1992.tb00868.x

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Identification of individual amino acids required for secretion within the haemolysin (HlyA) C-terminal targeting region.PMID 1625577Read ↗

Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin.Semantic proximity Read ↗

Mutations affecting the extreme C terminus of Escherichia coli haemolysin A reduce haemolytic activity by altering the folding of the toxin.Semantic proximity Read ↗

Evidence that residues -15 to -46 of the haemolysin secretion signal are involved in early steps in secretion, leading to recognition of the translocator.Semantic proximity Read ↗

TolC, an Escherichia coli outer membrane protein required for hemolysin secretion.Semantic proximity Read ↗

In vivo and in vitro studies on interactions between the components of the hemolysin (HlyA) secretion machinery of Escherichia coli.Semantic proximity Read ↗

The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.Semantic proximity Read ↗

Optimisation of signal peptide for recombinant protein secretion in bacterial hosts.Semantic proximity Read ↗

Mutations affecting export and activity of cytolysin A from Escherichia coli.Semantic proximity Read ↗

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Tetratricopeptide repeats in the type III secretion chaperone, LcrH: their role in substrate binding and secretion.Semantic proximity Read ↗

Translocation and compartmentalization of Escherichia coli hemolysin (HlyA).Semantic proximity Read ↗

Equilibrium folding of pro-HlyA from Escherichia coli reveals a stable calcium ion dependent folding intermediate.Semantic proximity Read ↗

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