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| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Exhibition Hall 2+3 |
| Time |
10월 19일 (목요일) 11:00~12:30 |
| Code |
BIO.P-279 |
| Subject |
Zα domain of ADAR1 prefers to bind to Z-RNA better than Z-DNA |
| Authors |
Ae-Ree Lee, Joon-Hwa Lee*, Yeo-Jin Seo, Seo-Ree Choi
Department of Chemistry, Gyeongsang National University, Korea
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| Abstract |
Double-stranded RNA deaminase I (ADAR1) deaminates adenine in pre-mRNA to yield inosine (I), which codes as a guanine residue in mRNA. These A-to-I conversions can lead to functional changes in the resulting proteins. At its NH2-terminus, ADAR1 has two left-handed Z-DNA binding domains and preferentially binds Z-DNA, rather than B-DNA, with high binding affinity. The main difference between DNA and RNA is the presence of the ribose 2’-OH groups; however, this difference makes the two macromolecules very different with regard to their biochemical behavior as well as the structures they adopt as double helices. Both B-DNA and A-RNA can undergo a transition to left-handed double-helical structures, referred to as Z-DNA and Z-RNA. The crystal structural study of the Z-DNA binding domain of ADAR1 complexed to a r(CG)3 duplex RNA found that the Z-RNA helix is associated with a unique solvent pattern that distinguishes it from the otherwise similar conformation of Z-DNA.
In order to characterize the molecular recognition of Z-RNA by ADAR1, we performed NMR experiments with complexes of ADAR1 bound to r(CG)3 and these results were compared with those of Z-DNA, d(CG)3, induced by ADAR1 previously reported. We compared to the binding affinity of ZαADAR1 for both A-DNA and Z-DNA and characterized its A–Z transition activity.
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| E-mail |
dldofl24@naver.com |
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120th General Meeting of the KCS