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Article

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

Molecular microbiology - 1 Oct 1991

Stanley P, Koronakis V, Hughes C

Abstract excerpt

We have carried out an extensive mutational analysis of the C-terminal signal which targets the export of the 1024-residue haemolysin protein (HlyA) of Escherichia coli across both bacterial membranes into the surrounding medium. Over 60 variants of the HlyA C-terminal 53-amino-acid sequence were...

Topics

Amino Acid Sequence
Bacterial Proteins
Base Sequence
Cell Membrane
Chromosome Deletion
Cloning, Molecular
Escherichia coli
Escherichia coli Proteins
Genetic Variation
Hemolysin Proteins
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutagenesis, Site-Directed

Oligodeoxyribonucleotides

Protein Conformation

Protein Sorting Signals

Source

Identifiers

PMID: 1791754
DOI: 10.1111/j.1365-2958.1991.tb02085.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1791754-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin.PMID 1791754Read ↗

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

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 ↗

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

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

Characterization of the hlyB gene and its role in the production of the El Tor haemolysin of Vibrio cholerae O1.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 ↗

Characterization of the hemolysin transporter, HlyB, using an epitope insertion.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 ↗

Escherichia coli hemolysin mutants with altered target cell specificity.Semantic proximity Read ↗

A peptide derived from the putative transmembrane domain in the tail region of E. coli toxin hemolysin E assembles in phospholipid membrane and exhibits lytic activity to human red blood cells: plausible implications in the toxic activity of the protein.Semantic proximity Read ↗

Mutations affecting pore formation by haemolysin from Escherichia coli.Semantic proximity Read ↗

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