ArticleScientific reports2015
Molecular and structural analysis of Legionella DotI gives insights into an inner membrane complex essential for type IV secretion.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 43 citations in OpenAlex.
- Article
- Article
- Type IV secretion systems: reconciling diversity through a unified nomenclature.FEMS microbiology reviews · 2026Review
- Transmembrane effector substrates of type IV secretion systems: mechanisms of secretion and insertion into host cell membranes.microLife · 2026Review
- Inner membrane components of the plasmid pKM101 type IV secretion system TraE and TraD are DNA-binding proteins.Scientific reports · 2025Article
- Membrane association and polar localization of theProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Host-bacteria interactions: ecological and evolutionary insights from ancient, professional endosymbionts.FEMS microbiology reviews · 2024Review
- Blue Native PAGE Analysis of Bacterial Secretion Complexes.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Comparative Analysis of T4SS Molecular Architectures.Journal of microbiology and biotechnology · 2023Review
- Structure and Function of the Dot/Icm T4SS.bioRxiv : the preprint server for biology · 2023Article
- Host Adaptation in Legionellales Is 1.9 Ga, Coincident with Eukaryogenesis.Molecular biology and evolution · 2022Article
- Recent advances in structural studies of the Legionella pneumophila Dot/Icm type IV secretion system.Microbiology and immunology · 2022Review
- Proteins DotY and DotZ modulate the dynamics and localization of the type IVB coupling complex of Legionella pneumophila.Molecular microbiology · 2022Article
- Incompatibility Group I1 (IncI1) Plasmids: Their Genetics, Biology, and Public Health Relevance.Microbiology and molecular biology reviews : MMBR · 2021Review
- Structural and Biochemical Analysis of OrfG: The VirB8-like Component of the Conjugative Type IV Secretion System of ICEFrontiers in molecular biosciences · 2021Article
- Bacteria-Killing Type IV Secretion Systems.Frontiers in microbiology · 2019Review
- Characteristics of the Conjugative Transfer System of the IncM Plasmid pCTX-M3 and Identification of Its Putative Regulators.Journal of bacteriology · 2018Article
- VirB8 homolog TraE from plasmid pKM101 forms a hexameric ring structure and interacts with the VirB6 homolog TraD.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Polar delivery ofProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Type II Secretion Substrates ofmBio · 2017Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human pathogen Legionella pneumophila delivers a large array of the effector proteins into host cells using the Dot/Icm type IVB secretion system. Among the proteins composing the Dot/Icm system, an inner membrane protein DotI is known to be crucial for the secretion function but its structure and role in type IV secretion had not been elucidated. We report here the crystal structures of the periplasmic domains of DotI and its ortholog in the conjugation system of plasmid R64, TraM. These structures reveal a striking similarity to VirB8, a component of type IVA secretion systems, suggesting that DotI/TraM is the type IVB counterpart of VirB8. We further show that DotI and its partial paralog DotJ form a stable heterocomplex. R64 TraM, encoded by the conjugative plasmid lacking DotJ ortholog, forms a homo-hexamer. The DotI-DotJ complex is distinct from the core complex, which spans both inner and outer membranes to form a substrate conduit, and seems not to stably associate with the core complex. These results give insight into VirB8-family inner membrane proteins essential for type IV secretion and aid towards understanding the molecular basis of secretion systems essential for bacterial pathogenesis.
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