JKMRS Volume 24, No 4, pp 117, NMR Hydrogen Exchange Study of ... | |
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2020년 12월 20일 / 조회수: 534 | |
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,
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
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첨부파일 | 03-JKMRS_LeeJH.pdf |