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JKMRS Volume 24, No 4, pp 117, NMR Hydrogen Exchange Study of ...
2020년 12월 20일 / 조회수: 177

NMR Hydrogen Exchange Study of DNA Duplex Containing the Consensus Binding Site for Human MEIS1

 

Seo-Ree Choi, Ho-seong Jin, Yeo-Jin Seo and Joon-Hwa Lee*

 

 

Department of Chemistry and Research Institute of Natural Science, Gyeongsang National University, Jinju 52828,
Republic of Korea

 

 

 

 

Received Dec 3, 2020; Revised Dec 17, 2020; Accepted Dec 17, 2020

 


Abstract Transcription factors are proteins that bind specific sites or elements in regulatory regions of DNA, known as promoters or enhancers, where they control the transcription or expression of target genes. MEIS1 protein is a DNA-binding domain present in human transcription factors and plays important roles in various biological functions. The hydrogen exchange rate constants of the imino protons were determined for the wild-type containing the consensus DNA-binding site for the MEIS1 and those of the mutant DNA duplexes using NMR spectroscopy.  The G2A-, A3G- and C4T-mutant DNA duplexes lead to clear changes in thermal stabilities of these four consensus base pairs. These unique dynamic features of the four base pairs in the consensus 5'-TGAC-3' sequence might play crucial roles in the effective DNA binding of the MEIS1 protein.

 

 

Keywords NMR, DNA binding, Hydrogen exchange, MEIS1 transcription factor, Base-pair stability

 

* Address correspondence to: Joon-Hwa Lee, Department of Chemistry and Research Institute of Natural Science,Gyeongsang National University, Jinju 52828, Republic of Korea, Tel: 82-55-772-1490; Fax: 82-55-772-1489; E-mail:  joonhwa@gnu.ac.kr

 


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