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Supramolecular tholos-like architecture constituted by archaeal proteins without functional annotation
Maho Yagi-Utsumi1,2,3,4, Arunima Sikdar2,3, Chihong Song5
1Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Aichi, 444-8787, Japan.
Scientific Reports
|February 1, 2020
Summary
Archaeal proteasome chaperones PbaA and PbaB have distinct roles. This study reveals the PbaA/PF0014 complex
Area of Science:
- Structural Biology
- Biochemistry
- Microbiology
Background:
- Euryarchaeal genomes encode proteasome-assembling chaperone homologs PbaA and PbaB.
- Archaeal proteasome formation is chaperone-independent.
- PbaA forms a homopentamer and interacts with the unannotated protein PF0014.
Purpose of the Study:
- To elucidate the supramolecular structure of the PbaA/PF0014 complex.
- To understand the assembly and architecture of this archaeal protein complex.
Main Methods:
- Integrative structural analysis using native mass spectrometry.
- Solution scattering techniques.
- High-speed atomic force microscopy and electron microscopy.
Main Results:
- The PbaA/PF0014 complex is highly thermostable, composed of ten PbaA and ten PF0014 molecules.
- It forms a dumbbell-shaped structure with two PbaA homopentameric rings.
- A five-column tholos-like architecture with a central cavity was determined, potentially for biomacromolecule accommodation.
Conclusions:
- The PbaA/PF0014 complex exhibits a unique tholos-like architecture.
- Findings provide insights into Pba family protein functions.
- Offers a framework for designing novel protein cages.
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