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Structural analysis of septin 2, 6, and 7 complexes.
1Center for Cell Signaling, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA. ccl3j@virginia.edu
The Journal of Biological Chemistry
|August 18, 2006
Summary
Mammalian septins form filaments through unknown mechanisms. This study reveals septin interactions, suggesting polymerized filaments comprise laterally arranged core subunits, advancing our understanding of septin assembly.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Mammalian septins are GTP-binding proteins forming filaments.
- Septin filament assembly mechanisms remain poorly understood.
- Specific septin combinations hetero-oligomerize.
Purpose of the Study:
- To characterize the conformation of filamentous human septins (Sept2, Sept6, Sept7).
- To elucidate the interaction mechanisms between septin subunits.
- To understand the structural basis of septin filament formation.
Main Methods:
- Fluorescence resonance energy transfer (FRET).
- Size exclusion chromatography.
- Multi-angle light scattering (MALS).
Main Results:
- Sept6 and Sept7 interact via a parallel coiled-coil.
- Sept2 interacts with Sept6 through their C-terminal domains.
- Soluble, stable monomers and dimers of individual septins were produced.
Conclusions:
- The findings suggest a model for septin filament structure.
- Polymerized filaments may consist of laterally arranged septin core subunits.
- This provides insights into septin assembly and function.