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Structural and functional studies on stem cell transcription factors-an integrated in silico approach
- Subtitle
- in silico analysis of Oct4, Sox2 and Nanog
- Author(s)
- YESUDHAS DHANUSHA
- Advisor
- Sangdun Choi
- Department
- 일반대학원 분자과학기술학과
- Publisher
- The Graduate School, Ajou University
- Publication Year
- 2018-02
- Language
- eng
- Alternative Abstract
- Reprogramming of human somatic cells into induced pluripotent stem cells (iPSCs) signifies the advancement in biological principles and technologies that have been developed over the last decades [1]. The transcription factors (TFs) such as Oct4 and Sox2 and their interactions in biological systems are considered as the key factors in reprogramming process [2]. Despite the fact that Oct4 and Sox2 have independent roles in defining other cell types, their function in reprogramming cells is due to the cooperative interaction between them that drives the transcription of target genes [3, 4]. There are ample amount of biochemical studies available for these proteins, whereas structural mechanism behind their cooperative interactions are not clear. Explicit structural knowledge of protein-protein and protein-DNA interaction among Oct4, and Sox2 can support to analyze the structure-function relationship of these TFs and reprogramming process. The availability of Oct4 and Sox2 atomic structures has improved our understanding about their binding preferences [5-7]; however, there is no experimental evidence that shows how binding of one protein to DNA is necessary to incorporate other proteins, or what conformational alterations in DNA/protein perpetuate such allosteric mechanisms. Thus, in our first study we focused on Oct4/Sox2 cooperative interactions in undifferentiated embryonic cell transcription factor 1 (Utf1) and fibroblast growth factor 4 (Fgf4) promoter regions, in order to identify the structural mechanism behind its distinct efficiency during reprogramming process. TFs bind to DNA in a sequence-specific manner and function to regulate the transcription of target genes. Thus, it is valuable to study the unique characteristics of such specific DNA binding pattern for each TF. Hence, in our second study, the specificity and affinity of Sox2 protein for its distinct DNA binding patterns were analyzed using computational techniques.
- Fulltext
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- Graduate School of Ajou University > Department of Molecular Science and Technology > 4. Theses(Ph.D)
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