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대한화학회 제124회 학술발표회 및 총회 Base-pair opening dynamics study of nucleic acids by NMR spectroscopy

등록일
2019년 8월 19일 12시 05분 21초
접수번호
0381
발표코드
LIFE2-3 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 09시 : 40분
발표형식
심포지엄
발표분야
Life Chemistry - Light Irradiation Deep into Life-Science Chemistry
저자 및
공동저자
Joon-Hwa Lee
Department of Chemistry, Gyeongsang National University, Korea
Base-pair opening in nucleic acids is a structural fluctuation for proper conformational transitions that is required in their biological function. NMR hydrogen exchange experiment is one of widely used method to study the thermodynamics and kinetics for base-pair opening in nucleic acids. The hydrogen exchange data of imino protons are analyzed based on a two-state (open/closed) model for the base-pair, where hydrogen exchange only occurs from the open state. Here, we reported three base-pair opening dynamics studies which provide insights into the biological function of the interesting nucleic acids. First, a base-pair opening dynamics study was performed using model RNAs mimicking the cleavage site of wild type and B5 bulge-stabilizing mutant pri-miR156a constructs. This study suggests that the stabilities and/or opening dynamics of the C15·G98 and U16·A97 base-pairs at the cleavage site are essential for formation of the active conformation and for efficient processing of pri-miR156a, and that mutations of the B5 bulge can modulate mature miR156 levels as well as miR156-driven leaf number phenotypes via changes in the base-pair stability of the cleavage site. Second, the base-pair opening kinetics studies of three GATC-containing DNA duplexes found that two G·C base pairs of the hemimethylated GATC duplex displayed a faster base-pair opening rate and required less energy for the base-pair opening reaction than did those of the fully methylated one. Finally, the base-pair opening data of the P1 duplex of the Tetrahymena group I ribozyme revealed that three base pairs, U-1·G22, C-2·G23 and A2·U21 showed unusual base-pair opening thermodynamics which might be correlate with the undocking rates of the P1 helix into catalytic core.