TY  - JOUR
A1  - Altegoer, Florian
A1  - Quax, Tessa
A1  - Weiland, Paul
A1  - Nußbaum, Phillip
A1  - Giammarinaro, Pietro Ivan
A1  - Patro, Megha
A1  - Li, Zhengqun
A1  - Oesterhelt, Dieter
A1  - Grininger, Martin
A1  - Albers, Sonja Verena
A1  - Bange, Gert
T1  - Structural insights into the mechanism of archaellar rotational switching
T2  - Nature Communications
N2  - 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.
KW  - Biochemistry
KW  - Microbiology
Y1  - 2022
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/63260
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-632608
SN  - 2041-1723
N1  - The coordinates and structure factors generated in this study have been deposited in the PDB database under accession codes PDB-7OD9 and PDB-7OVP.
N1  - Open Access funding enabled and organized by Projekt DEAL.
VL  - 13
IS  - art. 2857
SP  - 1
EP  - 12
PB  - Nature Publishing Group
CY  - [London]
ER  -