ArticleJournal of molecular biology2015
The LcrG Tip Chaperone Protein of the Yersinia pestis Type III Secretion System Is Partially Folded.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Dynamic interaction of the Yersinia pseudotuberculosis type three secretion system proteins LcrV and LcrG.Protein science : a publication of the Protein Society · 2026Article
- Article
- Beyond Antibiotics: What the Future Holds.Antibiotics (Basel, Switzerland) · 2024Review
- Detergent headgroups control TolC folding in vitro.Biophysical journal · 2023Article
- Use of magnetic nanotrap particles in capturing Yersinia pestis virulence factors, nucleic acids and bacteria.Journal of nanobiotechnology · 2021Article
- TheMicroorganisms · 2021Review
- Molecular Targets and Strategies for Inhibition of the Bacterial Type III Secretion System (T3SS); Inhibitors Directly Binding to T3SS Components.Biomolecules · 2021Review
- The type III secretion system needle, tip, and translocon.Protein science : a publication of the Protein Society · 2019Review
- The Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cells.EcoSal Plus · 2019Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The type III secretion system (T3SS) is essential in the pathogenesis of Yersinia pestis, the causative agent of plague. A small protein, LcrG, functions as a chaperone to the tip protein LcrV, and the LcrG-LcrV interaction is important in regulating protein secretion through the T3SS. The atomic structure of the LcrG family is currently unknown. However, because of its predicted helical propensity, many have suggested that the LcrG family forms a coiled-coil structure. Here, we show by NMR and CD spectroscopy that LcrG lacks a tertiary structure and it consists of three partially folded α-helices spanning residues 7-38, 41-46, and 58-73. NMR titrations of LcrG with LcrV show that the entire length of a truncated LcrG (residues 7-73) is involved in binding to LcrV. However, there is regional variation in how LcrG binds to LcrV. The C-terminal region of a truncated LcrG (residues 52-73) shows tight binding interaction with LcrV while the N-terminal region (residues 7-51) shows weaker interaction with LcrV. This suggests that there are at least two binding events when LcrG binds to LcrV. Biological assays and mutagenesis indicate that the C-terminal region of LcrG (residues 52-73) is important in blocking protein secretion through the T3SS. Our results reveal structural and mechanistic insights into the atomic conformation of LcrG and how it binds to LcrV.
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