ArticleThe Journal of biological chemistry2010
The rate of folding dictates substrate secretion by the Escherichia coli hemolysin type 1 secretion system.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Bacterial lipid synthesizing enzymes PlsY and PlsC utilize both stereo-forms of glycerol-phosphate.EMBO reports · 2026Article
- Review
- Heat stress induces phage tolerance ineLife · 2025Article
- Enhanced secretion through type 1 secretion system by grafting a calcium-binding sequence to modify the folding of cargo proteins.Protein science : a publication of the Protein Society · 2025Article
- Not just passengers: effectors contribute to the assembly of the type VI secretion system as structural building blocks.Journal of bacteriology · 2025Review
- Article
- PySupercharge: a python algorithm for enabling ABC transporter bacterial secretion of all proteins through amino acid mutation.Microbial cell factories · 2024Article
- Export of Diverse and Bioactive Small Proteins through a Type I Secretion System.Applied and environmental microbiology · 2023Article
- Heterologously secreted MbxA from Moraxella bovis induces a membrane blebbing response of the human host cell.Scientific reports · 2022Article
- Generalized Approach towards Secretion-Based Protein Production via Neutralization of Secretion-Preventing Cationic Substrate Residues.International journal of molecular sciences · 2022Article
- Review
- Quantification and Surface Localization of the Hemolysin A Type I Secretion System at the Endogenous Level and under Conditions of Overexpression.Applied and environmental microbiology · 2022Article
- A hemolysin secretion pathway-based novel secretory expression platform for efficient manufacturing of tag peptides and anti-microbial peptides in Escherichia coli.Bioresources and bioprocessing · 2021Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Identity Determinants of the Translocation Signal for a Type 1 Secretion System.Frontiers in physiology · 2021Article
- Engineered Living Materials Based on Adhesin-Mediated Trapping of Programmable Cells.ACS synthetic biology · 2020Article
- Article
- Functional Reconstitution of HlyB, a Type I Secretion ABC Transporter, in Saposin-A Nanoparticles.Scientific reports · 2019Article
- Screening and purification of nanobodies from E. coli culture supernatants using the hemolysin secretion system.Microbial cell factories · 2019Article
- Type I Secretion Systems-One Mechanism for All?Microbiology spectrum · 2019Review
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Secretion of the Escherichia coli toxin hemolysin A (HlyA) is catalyzed by the membrane protein complex HlyB-HlyD-TolC and requires a secretion sequence located within the last 60 amino acids of HlyA. The Hly translocator complex exports a variety of passenger proteins when fused N-terminal to this secretion sequence. However, not all fusions are secreted efficiently. Here, we demonstrate that the maltose binding protein (MalE) lacking its natural export signal and fused to the HlyA secretion signal is poorly secreted by the Hly system. We anticipated that folding kinetics might be limiting secretion, and we therefore introduced the "folding" mutation Y283D. Indeed this mutant fusion protein was secreted at a much higher level. This level was further enhanced by the introduction of a second MalE folding mutation (V8G or A276G). Secretion did not require the molecular chaperone SecB. Folding analysis revealed that all mutations reduced the refolding rate of the substrate, whereas the unfolding rate was unaffected. Thus, the efficiency of secretion by the Hly system is dictated by the folding rate of the substrate. Moreover, we demonstrate that fusion proteins defective in export can be engineered for secretion while still retaining function.
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