Open AccessDNA-binding properties of FOXP3 transcription factor
Author(s) -
Jun Li,
Longying Jiang,
Xujun Liang,
Lingzhi Qu,
Daichao Wu,
Xiaojuan Chen,
Ming Guo,
Zhuchu Chen,
Lin Chen,
Yongheng Chen
Publication year - 2017
Publication title -
acta biochimica et biophysica sinica
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 0.771
H-Index - 57
eISSN - 1745-7270
pISSN - 1672-9145
DOI - 10.1093/abbs/gmx079
Subject(s) - transcription factor , dna , leucine zipper , dna binding protein , isothermal titration calorimetry , forkhead transcription factors , dna binding domain , biology , dna binding site , genetics , microbiology and biotechnology , chemistry , promoter , biochemistry , gene , gene expression
FOXP3, a lineage-specific forkhead (FKH) transcription factor, plays essential roles in the development and function of regulatory T cells. However, the DNA-binding properties of FOXP3 are not well understood. In this study, FOXP3 fragments containing different domains were purified, and their DNA-binding properties were investigated using electrophoretic mobility shift assay and isothermal titration calorimetry (ITC). Both the FKH and leucine-zipper domains were required for optimal DNA binding for FOXP3. FOXP3 protein not only binds with DNA sequences containing one FKH consensus sequence, but also binds with DNA sequences with two direct repeats of consensus sequences separated by three-nucleotides (DRE3). Our results shed lights on the mechanisms by which FOXP3 recognizes cognate DNA elements, and would facilitate further structural and functional studies of FOXP3.
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