ArticleStructure (London, England : 1993)2009
Structure and function of interacting IcmR-IcmQ domains from a type IVb secretion system in Legionella pneumophila.
Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Proteins DotY and DotZ modulate the dynamics and localization of the type IVB coupling complex of Legionella pneumophila.Molecular microbiology · 2022Article
- Evolutionary Dissection of the Dot/Icm System Based on Comparative Genomics of 58 Legionella Species.Genome biology and evolution · 2019Article
- IcmQ in the Type 4b secretion system contains an NAD+ binding domain.Structure (London, England : 1993) · 2013Article
- The arginine-rich N-terminal domain of ROP18 is necessary for vacuole targeting and virulence of Toxoplasma gondii.Cellular microbiology · 2012Article
- Type IVB Secretion Systems of Legionella and Other Gram-Negative Bacteria.Frontiers in microbiology · 2011Article
- Molecular pathogenesis of infections caused by Legionella pneumophila.Clinical microbiology reviews · 2010Review
- Biochemical characterization of three putative ATPases from a new type IV secretion system of Aeromonas veronii plasmid pAC3249A.BMC biochemistry · 2010Article
- Biological Diversity and Evolution of Type IV Secretion Systems.Current topics in microbiology and immunologyArticle
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
During infection, Legionella pneumophila creates a replication vacuole within eukaryotic cells and this requires a Type IVb secretion system (T4bSS). IcmQ plays a critical role in the translocase and associates with IcmR. In this paper, we show that the N-terminal domain of IcmQ (Qn) mediates self-dimerization, whereas the C-terminal domain with a basic linker promotes membrane association. In addition, the binding of IcmR to IcmQ prevents self-dimerization and also blocks membrane permeabilization. However, IcmR does not completely block membrane binding by IcmQ. We then determined crystal structures of Qn with the interacting region of IcmR. In this complex, each protein forms an alpha-helical hairpin within a parallel four-helix bundle. The amphipathic nature of helices in Qn suggests two possible models for membrane permeabilization by IcmQ. The Rm-Qn structure also suggests how IcmR-like proteins in other L. pneumophila species may interact with their IcmQ partners.
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