Atypical chemoreceptor arrays accommodate high membrane curvature

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 str...

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Published inNature communications Vol. 11; no. 1; pp. 5763 - 13
Main Authors Muok, Alise R., Ortega, Davi R., Kurniyati, Kurni, Yang, Wen, Maschmann, Zachary A., Sidi Mabrouk, Adam, Li, Chunhao, Crane, Brian R., Briegel, Ariane
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 13.11.2020
Nature Publishing Group
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Summary: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. The main components of the prokaryotic chemotaxis system, chemoreceptors, organize into a hexagonal (P6 symmetry) extended array. Here authors use cryo-ET and 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.
Bibliography:Dutch Research Council (NWO)
R35GM122535; R01AI078958; R01DE023080; P30 GM124165; S10 RR029205
USDOE Office of Science (SC)
European Union (EU)
National Institutes of Health (NIH)
National Institute of General Medical Sciences (NIGMS)
ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-020-19628-6