ReviewEcoSal Plus2016
Type I Protein Secretion-Deceptively Simple yet with a Wide Range of Mechanistic Variability across the Family.
Review in EcoSal Plus, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
35 citing papers in PubMed, 64 citations in OpenAlex.
- Potential Effects of Gut Microbiota in the Acute and Chronic Toxicity of Silver Nanoparticles toEnvironment & health (Washington, D.C.) · 2026Article
- Engineered Escherichia coli as a microbial cell factory for intracellular protein delivery: strains, vectors, mechanisms, and therapeutic applications.Microbial cell factories · 2026Review
- Review
- TXSelect: A multi-task learning model to identify secretory effectors.PLoS computational biology · 2025Article
- Ingestible optoelectronic capsules enable bidirectional communication with engineered microbes for controllable therapeutic interventions.Nature microbiology · 2025Article
- Acyl chains stabilize the acylated domain and determine the receptor-mediated interaction of the Bordetella adenylate cyclase toxin with cell membrane.The Journal of biological chemistry · 2025Article
- EXCRETE workflow enables deep proteomics of the microbial extracellular environment.Communications biology · 2024Article
- Type 1 secretion necessitates a tight interplay between all domains of the ABC transporter.Scientific reports · 2024Article
- Membrane Interaction Characteristics of the RTX Toxins and the Cholesterol-Dependence of Their Cytolytic/Cytotoxic Activity.International journal of molecular sciences · 2024Review
- A step forward to the optimized HlyA type 1 secretion system through directed evolution.Applied microbiology and biotechnology · 2023Article
- Optimized Hemolysin Type 1 Secretion System in Escherichia coli by Directed Evolution of the Hly Enhancer Fragment and Including a Terminator Region.Chembiochem : a European journal of chemical biology · 2022Article
- Review
- Investigations on the substrate binding sites of hemolysin B, an ABC transporter, of a type 1 secretion system.Frontiers in microbiology · 2022Article
- Analysis of HubP-dependent cell pole protein targeting in Vibrio cholerae uncovers novel motility regulators.PLoS genetics · 2022Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Dynamical nonequilibrium molecular dynamics reveals the structural basis for allostery and signal propagation in biomolecular systems.The European physical journal. B · 2021Review
- Proteomic Analyses ofFrontiers in cellular and infection microbiology · 2021Article
- Identity Determinants of the Translocation Signal for a Type 1 Secretion System.Frontiers in physiology · 2021Article
- Secrete or perish: The role of secretion systems inComputational and structural biotechnology journal · 2021Review
- RTX-Toxins.Toxins · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
A very large type I polypeptide begins to reel out from a ribosome; minutes later, the still unidentifiable polypeptide, largely lacking secondary structure, is now in some cases a thousand or more residues longer. Synthesis of the final hundred C-terminal residues commences. This includes the identity code, the secretion signal within the last 50 amino acids, designed to dock with a waiting ATP binding cassette (ABC) transporter. What happens next is the subject of this review, with the main, but not the only focus on hemolysin HlyA, an RTX protein toxin secreted by the type I system. Transport substrates range from small peptides to giant proteins produced by many pathogens. These molecules, without detectable cellular chaperones, overcome enormous barriers, crossing two membranes before final folding on the cell surface, involving a unique autocatalytic process.Unfolded HlyA is extruded posttranslationally, C-terminal first. The transenvelope "tunnel" is formed by HlyB (ABC transporter), HlyD (membrane fusion protein) straddling the inner membrane and periplasm and TolC (outer membrane). We present a new evaluation of the C-terminal secretion code, and the structure function of HlyD and HlyB at the heart of this nanomachine. Surprisingly, key details of the secretion mechanism are remarkably variable in the many type I secretion system subtypes. These include alternative folding processes, an apparently distinctive secretion code for each type I subfamily, and alternative forms of the ABC transporter; most remarkably, the ABC protein probably transports peptides or polypeptides by quite different mechanisms. Finally, we suggest a putative structure for the Hly-translocon, HlyB, the multijointed HlyD, and the TolC exit.
Indexed as
Identifiers
What OpenQuestion holds
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.