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Updated: Nov 30, 2025

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Atypical chemoreceptor arrays accommodate high membrane curvature
Alise R Muok1,2, Davi R Ortega3, Kurni Kurniyati4
1Institute for Biology, Leiden University, Sylviusweg 72, 2333 BE, Leiden, Netherlands.
Researchers discovered a new P2 symmetry in the prokaryotic chemotaxis system of Treponema denticola, differing from the previously known hexagonal P6 symmetry. This finding reveals novel molecular arrangements in highly curved membranes, expanding our understanding of cellular signaling diversity.
Area of Science:
- Microbiology
- Cellular Biology
- Structural Biology
Background:
- The prokaryotic chemotaxis system is a well-established signaling pathway crucial for bacterial motility and environmental sensing.
- Chemoreceptors in known systems typically form hexagonal (P6 symmetry) arrays, organizing the signaling machinery.
- High membrane curvature presents a challenge for the assembly of large protein arrays.
Purpose of the Study:
- To investigate the structural organization of the chemotaxis apparatus in Treponema denticola, a bacterium with highly curved membranes.
- To determine the symmetry and molecular arrangement of chemoreceptor arrays in T. denticola.
- To identify novel components or organizational principles within this prokaryotic signaling system.
Main Methods:
- Cryo-electron tomography (cryo-ET) was employed to visualize the native structure of the chemotaxis arrays.
- Analysis of protein organization, including the histidine kinase CheA, CheW, and CheR-like fusion proteins.
- Investigation of the role of the oxygen sensor ODP in array assembly.
Main Results:
- Identified a novel P2 symmetry in the T. denticola chemotaxis apparatus, distinct from the canonical P6 symmetry.
- Revealed a linear organization of the histidine kinase CheA, contributing to the P2 symmetry and accommodating high membrane curvature.
- Discovered atypical features including an extended CheA dimerization domain and a CheW-CheR-like fusion protein essential for array order.
- Demonstrated that the oxygen sensor ODP influences the ordering of CheA within the arrays.
Conclusions:
- The chemotaxis system in Treponema denticola exhibits a unique P2 symmetry, adapted for highly curved membranes.
- This discovery highlights a greater diversity in the structural organization and assembly of prokaryotic chemotaxis signaling arrays than previously recognized.
- The findings suggest novel evolutionary strategies for chemosensory systems in bacteria with distinct cellular morphologies.
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