Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

Haemolysin secretion from E coli.

I B Holland¹, B Kenny, M Blight

¹Department of Genetics, University of Leicester, UK.

|February 1, 1990

Summary

This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

The role of propeptide-mediated autoinhibition and intermolecular chaperone in the maturation of cognate catalytic domain in leucine aminopeptidase.

Journal of structural biology·2021

Same author

Knowledge translation: Radiographers compared to other healthcare professionals.

Radiography (London, England : 1995)·2020

Same author

Bacterial metabolic 'toxins': a new mechanism for lactose and food intolerance, and irritable bowel syndrome.

Toxicology·2010

Same author

Importance of eps genes from Bacillus subtilis in biofilm formation and swarming.

Journal of applied genetics·2010

Same author

Poly(3-hydroxybutyrate-co-3-hydroxyvalerate) composite biomaterials for bone tissue regeneration: in vitro performance assessed by osteoblast proliferation, osteoclast adhesion and resorption, and macrophage proinflammatory response.

Journal of biomedical materials research. Part A·2007

Same author

Verapamil, a Ca2+ channel inhibitor acts as a local anesthetic and induces the sigma E dependent extra-cytoplasmic stress response in E. coli.

Biochimica et biophysica acta·2006

Escherichia coli haemolysin (HlyA) secretion utilizes a novel C-terminal signal, directly transported to the medium via the HlyB/HlyD complex. This mechanism can be harnessed to secrete other proteins.

Area of Science:

Microbiology
Molecular Biology
Protein Secretion

Background:

Haemolysin (HlyA) is a toxin secreted by Escherichia coli.
Understanding bacterial secretion systems is crucial for molecular biology and medicine.

Purpose of the Study:

To review the structure, function, and regulation of the HlyA secretion mechanism in E. coli.
To highlight the novel C-terminal targeting signal of HlyA.
To discuss the role of HlyB and HlyD proteins in HlyA translocation.

Main Methods:

Review of existing literature on HlyA secretion.
Analysis of the HlyA C-terminal domain's role in secretion.
Examination of the HlyB/HlyD transenvelope complex function.

Related Experiment Videos

Main Results:

HlyA secretion is directed by a novel C-terminal signal (last 27-50 amino acids).
Secretion occurs directly to the medium without periplasmic intermediates or processing.
The HlyA C-terminal domain can mediate secretion of heterologous proteins.
HlyB and HlyD form a complex essential for HlyA translocation.
HlyB is related to ATP-dependent secretion proteins found in humans.

Conclusions:

The HlyA secretion system represents a unique mechanism for protein export.
The HlyB/HlyD complex functions as a transenvelope secretion machine.
The HlyA secretion pathway has potential applications for heterologous protein delivery.