ReviewJournal of bioenergetics and biomembranes1990
The mechanism of secretion of hemolysin and other polypeptides from gram-negative bacteria.
Review in Journal of bioenergetics and biomembranes, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed, 82 citations in OpenAlex.
- Uncommon Pathogens in Common Presentations: Genetic Profiling and Virulence Determinants ofInfectious disease reports · 2025Article
- Review
- Article
- The rate of folding dictates substrate secretion by the Escherichia coli hemolysin type 1 secretion system.The Journal of biological chemistry · 2010Article
- Fusobacterium nucleatum outer membrane proteins Fap2 and RadD induce cell death in human lymphocytes.Infection and immunity · 2010Article
- Metabolic shutdown in Escherichia coli cells lacking the outer membrane channel TolC.Molecular microbiology · 2010Article
- Multicomponent drug efflux complexes: architecture and mechanism of assembly.Future microbiology · 2009Review
- Mutations in HlyD, part of the type 1 translocator for hemolysin secretion, affect the folding of the secreted toxin.Journal of bacteriology · 2005Article
- Characterization of the avian pathogenic Escherichia coli hemagglutinin Tsh, a member of the immunoglobulin A protease-type family of autotransporters.Infection and immunity · 1999Article
- The interleukin-1 beta-converting enzyme (ICE) is localized on the external cell surface membranes and in the cytoplasmic ground substance of human monocytes by immuno-electron microscopy.The Journal of experimental medicine · 1995Article
- Genetic analysis of the colicin V secretion pathway.Genetics · 1995Article
- Isolation and characterization of a second exe operon required for extracellular protein secretion in Aeromonas hydrophila.Journal of bacteriology · 1994Article
- Genetic map of the Actinobacillus pleuropneumoniae RTX-toxin (Apx) operons: characterization of the ApxIII operons.Infection and immunity · 1994Article
- ABC transporters: bacterial exporters.Microbiological reviews · 1993Review
- Hemin uptake in Porphyromonas gingivalis: Omp26 is a hemin-binding surface protein.Journal of bacteriology · 1993Article
- Association of Actinobacillus actinomycetemcomitans leukotoxin with nucleic acids on the bacterial cell surface.Infection and immunity · 1993Article
- Isolation and analysis of eight exe genes and their involvement in extracellular protein secretion and outer membrane assembly in Aeromonas hydrophila.Journal of bacteriology · 1993Article
- Structural analysis of the Actinobacillus pleuropneumoniae-RTX-toxin I (ApxI) operon.Infection and immunity · 1993Article
- Subcellular localization of seven VirB proteins of Agrobacterium tumefaciens: implications for the formation of a T-DNA transport structure.Journal of bacteriology · 1993Article
- A patch-clamp investigation of the Streptococcus faecalis cell membrane.The Journal of membrane biology · 1993Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the secretion of polypeptides from Gram-negative bacteria, the outer membrane constitutes a specific barrier which has to be circumvented. In the majority of systems, secretion is a two-step process, with initial export to the periplasm involving an N-terminal signal sequence. Transport across the outer membrane then involves a variable number of ancillary polypeptides including both periplasmic and outer membrane. While such ancillary proteins are probably specific for each secreted protein, the mechanism of movement across the outer membrane is unknown. In contrast to these systems, secretion of the E. coli hemolysin (HlyA) has several distinctive features. These include a novel targeting signal located within the last 50 or so C-terminal amino acids, the absence of any periplasmic intermediates in transfer, and a specific membrane-bound translocator, HlyB, with important mammalian homologues such as P-glycoprotein (Mdr) and the cystic fibrosis protein. In this review we discuss the nature of the HlyA targeting signal, the structure and function of HlyB, and the probability that HlyA is secreted directly to the medium through a trans-envelope complex composed of HlyB and HlyD.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.