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Atypical chemoreceptor arrays accommodate high membrane curvature

Alise R. Muok, Davi R. Ortega, Kurni Kurniyati, Wen Yang, Zachary A. Maschmann, Adam Sidi Mabrouk, Chunhao Li, Brian R. Crane and Ariane Briegel ()
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Alise R. Muok: Leiden University
Davi R. Ortega: Department of Biology, California Institute of Technology
Kurni Kurniyati: Virginia Commonwealth University
Wen Yang: Leiden University
Zachary A. Maschmann: Cornell University
Adam Sidi Mabrouk: Leiden University
Chunhao Li: Virginia Commonwealth University
Brian R. Crane: Cornell University
Ariane Briegel: Leiden University

Nature Communications, 2020, vol. 11, issue 1, 1-13

Abstract: Abstract The prokaryotic chemotaxis system is arguably the best-understood signaling pathway in biology. In all previously described species, chemoreceptors organize into a hexagonal (P6 symmetry) extended array. Here, we report an alternative symmetry (P2) of the chemotaxis apparatus that emerges from a strict linear organization of the histidine kinase CheA in Treponema denticola cells, which possesses arrays with the highest native curvature investigated thus far. Using cryo-ET, we reveal that Td chemoreceptor arrays assume an unusual arrangement of the supra-molecular protein assembly that has likely evolved to accommodate the high membrane curvature. The arrays have several atypical features, such as an extended dimerization domain of CheA and a variant CheW-CheR-like fusion protein that is critical for maintaining an ordered chemosensory apparatus. Furthermore, the previously characterized Td oxygen sensor ODP influences CheA ordering. These results suggest a greater diversity of the chemotaxis signaling system than previously thought.

Date: 2020
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DOI: 10.1038/s41467-020-19628-6

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