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제108회 대한화학회 학술발표회, 총회 및 기기전시회 안내 NMR study on the B-Z junction DNA complexed with Z-DNA binding domain of human ADAR1 protein: implication for initiation of sequence-specific B-Z transition in a long DNA duplex

등록일
2011년 8월 1일 12시 58분 33초
접수번호
1030
발표코드
Ⅰ-BIO.P-205 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅰ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
박진완, 이준화
경상대학교 화학과, Korea
The human RNA editing enzyme, ADAR1 (double-stranded RNA deaminase I), deaminates adenine in pre-mRNA to yield inosine which codes as guanine. ADAR1 has two left-handed Z-DNA binding domains, Zα and Zβ, at its NH2-terminus and preferentially binds Z-DNA, rather than B-DNA, with high binding affinity. Left-handed Z-DNA is a higher-energy form of the double helix produced at an alternating CG sequence region and is stabilized by high salt concentration or negative super-coiling. Recently, X-ray crystal structure of the B-Z junction induced by the Z-DNA binding protein, where the alternating CGCGCG exhibited left-handed Z-DNA whereas a non-alternating AT-rich region maintained B-form helix, was reported. They also found the continuous stacking of bases between B-DNA and Z-DNA segments with the breaking of one base pair at the junction. This result indicates that the one base pair at the B-Z junction DNA should be destabilized and then its bases might be extruded to allow the B-Z conformational change at the CGCGCG region. Z-form junctions at solution state shows that base extrusion occurs not only at the DNA B?Z junction, but also at the RNA A?Z and DNA Z?Z junctions. In order to characterize the molecular mechanism in formation of B-Z junction DNA, we performed NMR experiments with complexes of ZαADAR1 bound to B-Z junction DNA produced at a variety of protein-to-DNA molar ratios. These results provide insight into the molecular mechanism on the formation of B-Z junction DNA induced by ZαADAR1

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