Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 DNA-binding properties of FOXP3 transcription factor.

Literature DB >> 28910978

DNA-binding properties of FOXP3 transcription factor.

Jun Li^1,2, Longying Jiang¹, Xujun Liang¹, Lingzhi Qu¹, Daichao Wu¹, Xiaojuan Chen^1,2, Ming Guo¹, Zhuchu Chen^1,3, Lin Chen^1,4, Yongheng Chen^1,2,3.

Abstract

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.

© The Author 2017. Published by Oxford University Press on behalf of the Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.

Entities: Gene

Keywords: DNA binding; FOXP3; electrophoretic mobility shift assay; isothermal titration calorimetry; protein purification

Mesh：

Substances：

Year: 2017 PMID： 28910978 PMCID： PMC6276865 DOI： 10.1093/abbs/gmx079

Source DB: PubMed Journal: Acta Biochim Biophys Sin (Shanghai) ISSN： 1672-9145 Impact factor: 3.848

27 in total

1. Structural and biological features of FOXP3 dimerization relevant to regulatory T cell function.

Authors: Xiaomin Song; Bin Li; Yan Xiao; Chunxia Chen; Qiang Wang; Yujie Liu; Alan Berezov; Chen Xu; Yayi Gao; Zhiyuan Li; Shiaw-Lin Wu; Zheng Cai; Hongtao Zhang; Barry L Karger; Wayne W Hancock; Andrew D Wells; Zhaocai Zhou; Mark I Greene
Journal: Cell Rep Date: 2012-06-15 Impact factor: 9.423

2. Intranuclear interactomic inhibition of FoxP3 suppresses functions of Treg cells.

Authors: Jong-Hyun Park; Ji Seung Ko; Yoonchul Shin; Jen Young Cho; Han-ah Oh; Alfred L M Bothwell; Alfred M Bothwell; Sang-Kyou Lee
Journal: Biochem Biophys Res Commun Date: 2014-07-17 Impact factor: 3.575

3. Foxp3 controls regulatory T-cell function by interacting with AML1/Runx1.

Authors: Masahiro Ono; Hiroko Yaguchi; Naganari Ohkura; Issay Kitabayashi; Yuko Nagamura; Takashi Nomura; Yoshiki Miyachi; Toshihiko Tsukada; Shimon Sakaguchi
Journal: Nature Date: 2007-03-21 Impact factor: 49.962

4. Genome-wide identification of human FOXP3 target genes in natural regulatory T cells.

Authors: Timothy J Sadlon; Bridget G Wilkinson; Stephen Pederson; Cheryl Y Brown; Suzanne Bresatz; Tessa Gargett; Elizabeth L Melville; Kaimen Peng; Richard J D'Andrea; Gary G Glonek; Gregory J Goodall; Heddy Zola; M Frances Shannon; Simon C Barry
Journal: J Immunol Date: 2010-06-16 Impact factor: 5.422

5. Deficiency in regulatory T cells results in development of antimitochondrial antibodies and autoimmune cholangitis.

Authors: Weici Zhang; Rahul Sharma; Shyr-Te Ju; Xiao-Song He; Yanyan Tao; Koichi Tsuneyama; Zhigang Tian; Zhe-Xiong Lian; Shu Man Fu; M Eric Gershwin
Journal: Hepatology Date: 2009-02 Impact factor: 17.425

6. The ability to enhance the solubility of its fusion partners is an intrinsic property of maltose-binding protein but their folding is either spontaneous or chaperone-mediated.

Authors: Sreejith Raran-Kurussi; David S Waugh
Journal: PLoS One Date: 2012-11-16 Impact factor: 3.240

7. Microfluidic affinity and ChIP-seq analyses converge on a conserved FOXP2-binding motif in chimp and human, which enables the detection of evolutionarily novel targets.

Authors: Christopher S Nelson; Chris K Fuller; Polly M Fordyce; Alexander L Greninger; Hao Li; Joseph L DeRisi
Journal: Nucleic Acids Res Date: 2013-04-26 Impact factor: 16.971

8. Structure of the FoxM1 DNA-recognition domain bound to a promoter sequence.

Authors: D R Littler; M Alvarez-Fernández; A Stein; R G Hibbert; T Heidebrecht; P Aloy; R H Medema; A Perrakis
Journal: Nucleic Acids Res Date: 2010-03-31 Impact factor: 16.971

9. Expression of proteins in Escherichia coli as fusions with maltose-binding protein to rescue non-expressed targets in a high-throughput protein-expression and purification pipeline.

Authors: Stephen N Hewitt; Ryan Choi; Angela Kelley; Gregory J Crowther; Alberto J Napuli; Wesley C Van Voorhis
Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Date: 2011-08-13

Review 5. Toward a mechanistic understanding of DNA binding by forkhead transcription factors and its perturbation by pathogenic mutations.

Authors: Shuyan Dai; Linzhi Qu; Jun Li; Yongheng Chen
Journal: Nucleic Acids Res Date: 2021-10-11 Impact factor: 16.971

5 in total

DNA-binding properties of FOXP3 transcription factor.

1. Structural and biological features of FOXP3 dimerization relevant to regulatory T cell function.

2. Intranuclear interactomic inhibition of FoxP3 suppresses functions of Treg cells.

3. Foxp3 controls regulatory T-cell function by interacting with AML1/Runx1.

4. Genome-wide identification of human FOXP3 target genes in natural regulatory T cells.

5. Deficiency in regulatory T cells results in development of antimitochondrial antibodies and autoimmune cholangitis.

6. The ability to enhance the solubility of its fusion partners is an intrinsic property of maltose-binding protein but their folding is either spontaneous or chaperone-mediated.

7. Microfluidic affinity and ChIP-seq analyses converge on a conserved FOXP2-binding motif in chimp and human, which enables the detection of evolutionarily novel targets.

8. Structure of the FoxM1 DNA-recognition domain bound to a promoter sequence.

9. Expression of proteins in Escherichia coli as fusions with maltose-binding protein to rescue non-expressed targets in a high-throughput protein-expression and purification pipeline.

10. Transcription factor Foxp3 and its protein partners form a complex regulatory network.

1. Structural basis of binding of homodimers of the nuclear receptor NR4A2 to selective Nur-responsive DNA elements.

2. Structural basis for DNA recognition by FOXC2.

Review 3. Post-Translational Regulations of Foxp3 in Treg Cells and Their Therapeutic Applications.

Review 4. The Importance of the Transcription Factor Foxp3 in the Development of Primary Immunodeficiencies.

Review 5. Toward a mechanistic understanding of DNA binding by forkhead transcription factors and its perturbation by pathogenic mutations.