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Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions
Published on: October 21, 2016
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Direct interaction between EFL1 and SBDS is mediated by an intrinsically disordered insertion domain
Nozomi Asano1, Haruka Atsuumi1, Akiyoshi Nakamura2
1Graduate School of Life Sciences, Hokkaido University, Sapporo 060-0810, Japan.
Biochemical and Biophysical Research Communications
|January 11, 2014
Summary
Elongation factor-like 1 (EFL1) and Shwachman-Bodian-Diamond syndrome (SBDS) protein directly interact, revealing their roles in ribosome maturation by removing the Tif6 (eIF6) anti-association factor.
Area of Science:
- Molecular Biology
- Protein Interactions
- Ribosome Biogenesis
Background:
- Ribosome maturation is essential for protein synthesis.
- Tif6 (eIF6) acts as an anti-association factor during ribosome assembly.
- Elongation factor-like 1 (EFL1) and Shwachman-Bodian-Diamond syndrome (SBDS) protein are implicated in Tif6 removal.
Purpose of the Study:
- To elucidate the mechanism of Tif6 dissociation mediated by EFL1 and SBDS.
- To characterize the direct interaction between EFL1 and SBDS.
Main Methods:
- Size exclusion chromatography
- Gel shift assay
- Isothermal titration calorimetry (ITC)
- Circular dichroism (CD) spectroscopy
Main Results:
- EFL1 directly interacts with SBDS.
- The EFL1 insertion domain and SBDS domains II-III are crucial for their interaction.
- SBDS binding induces a fixed conformation in the EFL1 insertion domain, previously unstructured.
Conclusions:
- EFL1 and SBDS form a complex to facilitate Tif6 removal from the ribosome.
- The conformational change in EFL1 upon SBDS binding is key to Tif6 dissociation.
- This study provides insights into the roles of EFL1 and SBDS in late-stage ribosome maturation.
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