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Updated: Jun 24, 2026

Applying Live Cell Imaging and Cryo-Electron Tomography to Resolve Spatiotemporal Features of the Legionella pneumophila Dot/Icm Secretion System
Published on: March 10, 2020
Structure and function of interacting IcmR-IcmQ domains from a type IVb secretion system in Legionella pneumophila
Suchismita Raychaudhury1, Jeremiah D Farelli, Timothy P Montminy
1Department of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118-2526, USA.
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.
Insights
Legionella pneumophila uses IcmQ to form a vacuole for replication. The protein IcmR inhibits IcmQ
Area of Science:
- Microbiology
- Cell Biology
- Structural Biology
Background:
- Legionella pneumophila infection relies on vacuole formation.
- The Type IVb secretion system (T4bSS) is essential for vacuole biogenesis.
- IcmQ is a key T4bSS component interacting with IcmR.
Purpose of the Study:
- To elucidate the structural and functional roles of IcmQ and its interaction with IcmR.
- To understand the mechanism of membrane association and permeabilization by IcmQ.
- To provide insights into IcmR-mediated regulation of IcmQ.
Main Methods:
- Protein domain analysis (N-terminal Qn, C-terminal domain, basic linker).
- Biochemical assays for self-dimerization and membrane association/permeabilization.
- Crystal structure determination of Qn in complex with IcmR.
Main Results:
- The N-terminal domain (Qn) of IcmQ mediates self-dimerization.
- The C-terminal domain and basic linker promote membrane association.
- IcmR binding inhibits IcmQ self-dimerization and membrane permeabilization but not membrane binding.
- Crystal structures reveal a four-helix bundle interaction between Qn and IcmR.
Conclusions:
- IcmQ self-dimerization and membrane permeabilization are regulated by IcmR.
- Structural data provides models for IcmQ-mediated membrane permeabilization.
- Insights into interspecies IcmQ-IcmR interactions in Legionella.
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