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Architecture of the yeast Elongator complex
Maria I Dauden1, Jan Kosinski1, Olga Kolaj-Robin2,3,4
1European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.
EMBO Reports
|December 16, 2016
Summary
The Elongator complex, crucial for tRNA modification and proteome stability, has had its structure elucidated. This study reveals its two-lobed scaffold formed by Elp1-3 subunits, providing a framework for understanding its function.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- The Elongator complex is vital for modifying tRNA wobble bases, ensuring proteome stability.
- This complex, comprising six subunits (Elp1-6), is essential for cellular homeostasis.
- The precise architecture and mechanism of Elongator have remained largely unknown.
Purpose of the Study:
- To determine the overall architecture of the yeast Elongator complex.
- To elucidate the structural basis of its tRNA modification activity.
- To provide a detailed structural framework for Elongator function.
Main Methods:
- Integrative structure determination.
- X-ray crystallography of the Elongator complex and Elp123 sub-complex.
- Biochemical analyses for validation.
Main Results:
- The structures of the fully assembled yeast Elongator and the Elp123 sub-complex were determined.
- A two-lobed scaffold formed by two copies each of Elp1, Elp2, and Elp3 subunits was identified.
- The Elp456 sub-complex binds asymmetrically to this scaffold.
Conclusions:
- The study presents a structural framework for the Elongator complex.
- This framework explains how Elongator carries out its essential tRNA modification activity.
- The findings are consistent with and validate previous biochemical data.
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