Native structure of a type IV secretion system core complex essential for Legionella pathogenesis.

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ID: 100105
2014
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Ranked #107 of 292 articles by views in Proceedings of the National Academy of Sciences of the United States of America

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Abstract
Bacterial type IV secretion systems are evolutionarily related to conjugation systems and play a pivotal role in infection by delivering numerous virulence factors into host cells. Using transmission electron microscopy, we report the native molecular structure of the core complex of the Dot/Icm type IV secretion system encoded by Legionella pneumophila, an intracellular human pathogen. The biochemically isolated core complex, composed of at least five proteins--DotC, DotD, DotF, DotG, and DotH--has a ring-shaped structure. Intriguingly, morphologically distinct premature complexes are formed in the absence of DotG or DotF. Our data suggest that DotG forms a central channel spanning inner and outer membranes. DotF, a component dispensable for type IV secretion, plays a role in efficient embedment of DotG into the functional core complex. These results highlight a common scheme for the biogenesis of transport machinery.
Reference Key
kubori2014nativeproceedings Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Kubori, Tomoko;Koike, Masafumi;Bui, Xuan Thanh;Higaki, Saori;Aizawa, Shin-Ichi;Nagai, Hiroki;
Journal Proceedings of the National Academy of Sciences of the United States of America
Year 2014
DOI
10.1073/pnas.1404506111
URL
Keywords
membrane proteins assembly pathway effector translocation nanomachine

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