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제124회 대한화학회 학술발표회, 총회 및 기기전시회 안내 NMR study of fusion protein Zα Domain of ADAR1 linked N-terminal domain of the vaccinia virus protein E3L

등록일
2019년 8월 27일 21시 57분 43초
접수번호
1666
발표코드
LIFE.P-225 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
10월 18일 (금요일) 11:00~12:30
발표형식
포스터
발표분야
Life Chemistry
저자 및
공동저자
Nahyun Kim, Joon-Hwa Lee1,*
Chemistry department, Gyeongsang National University, Korea
1Department of Chemistry, Gyeongsang National University, Korea
Left-handed Z-DNA, which is a polymer of alternating d(CG)n sequence, is a higher energy conformation than B-DNA. Z-DNA is induced by high salt, negative supercoiling, and complex formation with Z-DNA binding proteins. Z-DNA binding domains are found in the RNA editing enzyme (ADAR1) and DNA-dependent activator of IFN-regulatory factor (DAI) in vertebrates, the E3L protein of poxviruses. Recent NMR studies of the complex formed between ZaADAR1 and a 6-base-paired (6-bp) DNA duplex referred to as d(CG)3, have suggested an active B–Z transition mechanism, in which the ZaADAR1 protein first binds to B-DNA and then converts it to left-handed Z-DNA, a conformation that is subsequently stabilized by the additional binding of a second ZaADAR1 molecule. All poxviruses have a gene called E3L that is essential for pathogenesis in the vaccinia virus. The E3L protein consists of two domains: an N-terminal Z-DNA binding domain and a C-terminal RNA binding domain. This N-terminal region shows sequence homology to the Za domains found in human ADAR1 (hZaADAR1). The Z-DNA binding affinity of the Za domain of E3L is required for viral pathogenicity. Here, to investigate the molecular mechanism of the B–Z transition of a DNA duplex induced by the fusion protein ZaADAR1+E3L(ZaA+E), we have conjoined a ZaADAR1 with ZaE3L and performed NMR hydrogen exchange experiments on the complexes formed by ZaA+E and d(CG)6 with a variety of protein-to-DNA (P/N) molar ratios. Comparison of these results with those from the analysis of hZaADAR1–d(CG)3 and ZaE3L-d(CG)3 in a previous study leads to valuable insights into the molecular mechanism of the B–Z transition of a DNA duplex induced by the fusion protein.

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