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Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
Published on: November 7, 2013
Co-operation between different targeting pathways during integration of a membrane protein
Rebecca Keller1, Jeanine de Keyzer, Arnold J M Driessen
1Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee, Scotland, UK.
The Journal of Cell Biology
|October 10, 2012
Summary
Membrane protein assembly in Streptomyces coelicolor involves both Sec and twin arginine transport (Tat) pathways. This study reveals their cooperation for correct Rieske protein folding and membrane integration.
Area of Science:
- Cellular biology
- Protein biogenesis
- Membrane protein assembly
Background:
- Rieske iron-sulfur protein is crucial for cytochrome bc1 and b6f complexes.
- It's typically exported via the twin arginine transport (Tat) pathway.
- In actinobacteria, Rieske protein is polytopic with three transmembrane domains.
Purpose of the Study:
- Investigate the assembly mechanism of the polytopic Rieske protein in Streptomyces coelicolor.
- Determine the roles of the Sec and Tat pathways in this process.
Main Methods:
- Genetic analysis
- Biochemical approaches
- Investigating protein integration and folding.
Main Results:
- The first two transmembrane domains integrate via the Sec pathway.
- The third transmembrane domain and proper iron-sulfur domain orientation require the Tat pathway.
- Demonstrated a novel cooperation between Sec and Tat systems.
Conclusions:
- The assembly of the Streptomyces coelicolor Rieske protein is a complex, multi-pathway process.
- Unprecedented co-operation between Sec and Tat pathways is essential for integral membrane protein assembly.
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