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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Muok AR,Ortega DR,Kurniyati K,Yang W,Maschmann ZA,Sidi Mabrouk A,Li C,Crane BR,Briegel Adoi
10.1038/s41467-020-19628-6subject
Has Abstractpub_date
2020-11-13 00:00:00pages
5763issue
1issn
2041-1723pii
10.1038/s41467-020-19628-6journal_volume
11pub_type
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