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Updated: Jul 27, 2026

Prediction and Validation of Gene Regulatory Elements Activated During Retinoic Acid Induced Embryonic Stem Cell Differentiation
Published on: June 21, 2016
The autoimmune regulator (AIRE) is a DNA-binding protein
P G Kumar1, M Laloraya, C Y Wang
1Department of Pathology, Immunology, and Laboratory Medicine, Center for Mammalian Genetics and Diabetes Center of Excellence, College of Medicine, University of Florida, Gainesville, Florida 32610, USA.
The autoimmune regulator (AIRE) protein forms dimers and tetramers, binding to specific DNA sequences. This DNA binding ability highlights AIRE's crucial role in immune system regulation.
Area of Science:
- Molecular Biology
- Immunology
- Genetics
Background:
- The autoimmune regulator (AIRE) protein is a key transcription regulator.
- AIRE possesses DNA-binding domains (zinc fingers, SAND domain) and nuclear receptor interaction motifs (LXXLL).
Purpose of the Study:
- To investigate the oligomerization and DNA-binding properties of the AIRE protein.
- To determine the role of phosphorylation in AIRE's function.
- To identify specific DNA motifs recognized by AIRE.
Main Methods:
- In vitro recombinant protein expression and purification.
- Electrophoretic mobility shift assays (EMSAs) to study DNA binding.
- Phosphorylation assays using protein kinase A and C.
- Competition assays to determine DNA binding affinity.
Main Results:
- Recombinant AIRE forms homodimers and homotetramers in vitro, also detected in thymic extracts.
- Phosphorylation by PKA and PKC induces AIRE oligomerization.
- AIRE dimers and tetramers bind to specific DNA sequences (G-doublets with ATTGGTTA and TTATTA-box).
- High binding affinity observed for sequences with TTATTA and tandem ATTGGTTA repeats.
Conclusions:
- AIRE functions as an oligomeric DNA-binding molecule.
- Phosphorylation regulates AIRE's oligomerization and DNA-binding capacity.
- AIRE plays a significant role in immune regulation through DNA binding.
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