NMR dynamics study of the Z-DNA binding domain of human ADAR1 bound to various DNA duplexes.
The Z-DNA binding domain of human ADAR1 (Zα(ADAR1)) preferentially binds Z-DNA rather than B-DNA with high binding affinity. Here, we have carried out chemical shift perturbation and backbone dynamics studies of Zα(ADAR1) in the free form and in complex with three DNA duplexes, d(CGCGCG)(2), d(CACGTG)(2), and d(CGTACG)(2). This study reveals that Zα(ADAR1) initially binds to d(CGCGCG)(2) through the distinct conformation, especially in the unusually flexible β1-loop-α2 region, from the d(CGCGCG)(2)-(Zα(ADAR1))(2) complex. This study also suggests that Zα(ADAR1) exhibits a distinct conformational change during the B-Z transition of non-CG-repeat DNA duplexes with low binding affinities compared to the CG-repeat DNA duplex.
Department of Chemistry and RINS, Gyeongsang National University, Jinju, Gyeongnam 660-701, Republic of Korea.
Ae-Ree
AR
Lee
Hee-Eun
HE
Kim
Yeon-Mi
YM
Lee
Minjee
M
Jeong
Kwang-Ho
KH
Choi
Jin-Wan
JW
Park
Yong-Geun
YG
Choi
Hee-Chul
HC
Ahn
Byong-Seok
BS
Choi
Joon-Hwa
JH
Lee
D000243:Adenosine Deaminase / Q000737:chemistry*; D000595:Amino Acid Sequence; D018899:CpG Islands; D059371:DNA, B-Form / Q000737:chemistry; D043542:DNA, Z-Form / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D016601:RNA-Binding Proteins; D012091:Repetitive Sequences, Nucleic Acid
D059371:DNA, B-Form; D043542:DNA, Z-Form; D016601:RNA-Binding Proteins; C567955:ADARB1 protein, human; D000243:Adenosine Deaminase