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Structural basis for LEAFY floral switch function and similarity with helix-turn-helix proteins
Cécile Hamès1, Denis Ptchelkine, Clemens Grimm
1Laboratoire Physiologie Cellulaire Végétale, UMR5168, Centre National de la Recherche Scientifique, Commissariat à l'énergie atomique, Institut National de la Recherche Agronomique, Université Joseph Fourier, Grenoble, France.
The EMBO Journal
|September 12, 2008
Summary
The LEAFY (LFY) protein
Area of Science:
- Plant biology
- Molecular genetics
- Evolutionary biology
Background:
- The LEAFY (LFY) protein is crucial for flower development in plants.
- Its precise molecular function in regulating floral transitions and gene expression remains unclear.
Purpose of the Study:
- To elucidate the molecular mechanism of LFY's function in floral development.
- To determine the DNA-binding mode and structural basis of LFY's regulatory activity.
Main Methods:
- X-ray crystallography was used to determine the structure of the Arabidopsis thaliana LFY DNA-binding domain.
- Structural analysis of LFY bound to target promoter DNA sequences.
Main Results:
- The crystal structure revealed LFY adopts a novel seven-helix fold.
- LFY binds DNA as a cooperative dimer, utilizing base-specific contacts in major and minor grooves.
- Structural similarity was found between LFY and helix-turn-helix proteins, including homeodomain proteins.
Conclusions:
- The cooperative dimerization mechanism of LFY binding likely explains its role in sharp developmental transitions.
- This structural insight provides a framework for understanding floral development and LFY's evolutionary significance.
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