Florian Altegoer, Tessa Quax, Paul Weiland, Phillip Nußbaum, Pietro Ivan Giammarinaro, Megha Patro, Zhengqun Li, Dieter Oesterhelt, Martin Grininger, Sonja Verena Albers, Gert Bange
- Signal transduction via phosphorylated CheY towards the flagellum and the archaellum involves a conserved mechanism of CheY phosphorylation and subsequent conformational changes within CheY. This mechanism is conserved among bacteria and archaea, despite substantial differences in the composition and architecture of archaellum and flagellum, respectively. Phosphorylated CheY has higher affinity towards the bacterial C-ring and its binding leads to conformational changes in the flagellar motor and subsequent rotational switching of the flagellum. In archaea, the adaptor protein CheF resides at the cytoplasmic face of the archaeal C-ring formed by the proteins ArlCDE and interacts with phosphorylated CheY. While the mechanism of CheY binding to the C-ring is well-studied in bacteria, the role of CheF in archaea remains enigmatic and mechanistic insights are absent. Here, we have determined the atomic structures of CheF alone and in complex with activated CheY by X-ray crystallography. CheF forms an elongated dimer with a twisted architecture. We show that CheY binds to the C-terminal tail domain of CheF leading to slight conformational changes within CheF. Our structural, biochemical and genetic analyses reveal the mechanistic basis for CheY binding to CheF and allow us to propose a model for rotational switching of the archaellum.
MetadatenAuthor: | Florian AltegoerORCiDGND, Tessa QuaxORCiDGND, Paul WeilandORCiD, Phillip NußbaumGND, Pietro Ivan GiammarinaroORCiD, Megha Patro, Zhengqun LiORCiDGND, Dieter OesterheltGND, Martin GriningerORCiDGND, Sonja Verena AlbersORCiDGND, Gert BangeORCiDGND |
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URN: | urn:nbn:de:hebis:30:3-632608 |
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DOI: | https://doi.org/10.1038/s41467-022-30358-9 |
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ISSN: | 2041-1723 |
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Parent Title (English): | Nature Communications |
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Publisher: | Nature Publishing Group |
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Place of publication: | [London] |
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Document Type: | Article |
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Language: | English |
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Date of Publication (online): | 2022/05/23 |
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Date of first Publication: | 2022/05/23 |
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Publishing Institution: | Universitätsbibliothek Johann Christian Senckenberg |
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Release Date: | 2023/01/17 |
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Tag: | Biochemistry; Microbiology |
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Volume: | 13 |
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Issue: | art. 2857 |
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Article Number: | 2857 |
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Page Number: | 12 |
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First Page: | 1 |
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Last Page: | 12 |
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Note: | The coordinates and structure factors generated in this study have been deposited in the PDB database under accession codes PDB-7OD9 and PDB-7OVP. |
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Note: | Open Access funding enabled and organized by Projekt DEAL. |
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HeBIS-PPN: | 505635682 |
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Institutes: | Biochemie, Chemie und Pharmazie |
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Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
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Sammlungen: | Universitätspublikationen |
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Licence (German): | Creative Commons - CC BY - Namensnennung 4.0 International |
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