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Genes 2017, 8(8), 192; doi:10.3390/genes8080192

Proteins Recognizing DNA: Structural Uniqueness and Versatility of DNA-Binding Domains in Stem Cell Transcription Factors

Department of Molecular Science and Technology, Ajou University, Suwon 443-749, Korea
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Received: 10 May 2017 / Revised: 22 July 2017 / Accepted: 25 July 2017 / Published: 1 August 2017
(This article belongs to the Special Issue Protein-DNA Interactions)
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Abstract

Proteins in the form of transcription factors (TFs) bind to specific DNA sites that regulate cell growth, differentiation, and cell development. The interactions between proteins and DNA are important toward maintaining and expressing genetic information. Without knowing TFs structures and DNA-binding properties, it is difficult to completely understand the mechanisms by which genetic information is transferred between DNA and proteins. The increasing availability of structural data on protein-DNA complexes and recognition mechanisms provides deeper insights into the nature of protein-DNA interactions and therefore, allows their manipulation. TFs utilize different mechanisms to recognize their cognate DNA (direct and indirect readouts). In this review, we focus on these recognition mechanisms as well as on the analysis of the DNA-binding domains of stem cell TFs, discussing the relative role of various amino acids toward facilitating such interactions. Unveiling such mechanisms will improve our understanding of the molecular pathways through which TFs are involved in repressing and activating gene expression. View Full-Text
Keywords: base and shape readouts; protein-DNA interaction; protein-DNA recognition; TF domain family base and shape readouts; protein-DNA interaction; protein-DNA recognition; TF domain family
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Yesudhas, D.; Batool, M.; Anwar, M.A.; Panneerselvam, S.; Choi, S. Proteins Recognizing DNA: Structural Uniqueness and Versatility of DNA-Binding Domains in Stem Cell Transcription Factors. Genes 2017, 8, 192.

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