Novel interaction of the z-dna binding domain of human ADAR1 with the oncogenic c-Myc promoter g-quadruplex. Kang, H., Le, T. V. T., Kim, K., Hur, J., Kim, K. K., & Park, H. Journal of molecular biology, 426(14):2594–2604, 2014. Publisher: Elsevier Ltd
Paper doi abstract bibtex Both G-quadruplex and Z-DNA can be formed in G-rich and repetitive sequences on genome, and their formation and biological functions are controlled by specific proteins. Z-DNA binding proteins, such as human ADAR1, have a highly conserved Z-DNA binding domain having selective affinity to Z-DNA. Here, our study identifies the Z-DNA binding domain of human ADAR1 (hZαADAR1) as a novel G-quadruplex binding protein that recognizes c-myc promoter G-quadruplex formed in NHEIII1 region and represses the gene expression. An electrophoretic migration shift assay shows the binding of hZαADAR1 to the intramolecular c-myc promoter G-quadruplex-forming DNA oligomer. To corroborate the binding of hZαADAR1 to the G-quadruplex, CD and NMR chemical shift perturbation analyses were conducted. CD results indicate that hZαADAR1 stabilizes the parallel-stranded conformation of the c-myc G-quadruplex. The NMR chemical shift perturbation data reveals that the G-quadruplex binding region in hZαADAR1 was almost identical to the Z-DNA binding region. Finally, promoter assay and western blot analysis show that hZαADAR1 suppresses the c-myc expression promoted by NHEIII1 region containing the G-quadruplex forming sequence. This finding suggests a novel function of Z-DNA-binding protein as a regulator of G-quadruplex-mediated gene expression.
@article{Kang2014,
title = {Novel interaction of the z-dna binding domain of human {ADAR1} with the oncogenic c-{Myc} promoter g-quadruplex.},
volume = {426},
issn = {1089-8638},
url = {http://www.sciencedirect.com/science/article/pii/S0022283614002289},
doi = {10.1016/j.jmb.2014.05.001},
abstract = {Both G-quadruplex and Z-DNA can be formed in G-rich and repetitive sequences on genome, and their formation and biological functions are controlled by specific proteins. Z-DNA binding proteins, such as human ADAR1, have a highly conserved Z-DNA binding domain having selective affinity to Z-DNA. Here, our study identifies the Z-DNA binding domain of human ADAR1 (hZαADAR1) as a novel G-quadruplex binding protein that recognizes c-myc promoter G-quadruplex formed in NHEIII1 region and represses the gene expression. An electrophoretic migration shift assay shows the binding of hZαADAR1 to the intramolecular c-myc promoter G-quadruplex-forming DNA oligomer. To corroborate the binding of hZαADAR1 to the G-quadruplex, CD and NMR chemical shift perturbation analyses were conducted. CD results indicate that hZαADAR1 stabilizes the parallel-stranded conformation of the c-myc G-quadruplex. The NMR chemical shift perturbation data reveals that the G-quadruplex binding region in hZαADAR1 was almost identical to the Z-DNA binding region. Finally, promoter assay and western blot analysis show that hZαADAR1 suppresses the c-myc expression promoted by NHEIII1 region containing the G-quadruplex forming sequence. This finding suggests a novel function of Z-DNA-binding protein as a regulator of G-quadruplex-mediated gene expression.},
number = {14},
journal = {Journal of molecular biology},
author = {Kang, Hyun-Jin and Le, Tuong Vy Thi and Kim, Kyungmin and Hur, Jeonghwan and Kim, Kyeong Kyu and Park, Hyun-Ju},
year = {2014},
pmid = {24813121},
note = {Publisher: Elsevier Ltd},
keywords = {\#nosource, Z-DNA binding domain of human ADAR1, c-Myc G-Quadruplex},
pages = {2594--2604},
}
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Here, our study identifies the Z-DNA binding domain of human ADAR1 (hZαADAR1) as a novel G-quadruplex binding protein that recognizes c-myc promoter G-quadruplex formed in NHEIII1 region and represses the gene expression. An electrophoretic migration shift assay shows the binding of hZαADAR1 to the intramolecular c-myc promoter G-quadruplex-forming DNA oligomer. To corroborate the binding of hZαADAR1 to the G-quadruplex, CD and NMR chemical shift perturbation analyses were conducted. CD results indicate that hZαADAR1 stabilizes the parallel-stranded conformation of the c-myc G-quadruplex. The NMR chemical shift perturbation data reveals that the G-quadruplex binding region in hZαADAR1 was almost identical to the Z-DNA binding region. Finally, promoter assay and western blot analysis show that hZαADAR1 suppresses the c-myc expression promoted by NHEIII1 region containing the G-quadruplex forming sequence. 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Z-DNA binding proteins, such as human ADAR1, have a highly conserved Z-DNA binding domain having selective affinity to Z-DNA. Here, our study identifies the Z-DNA binding domain of human ADAR1 (hZαADAR1) as a novel G-quadruplex binding protein that recognizes c-myc promoter G-quadruplex formed in NHEIII1 region and represses the gene expression. An electrophoretic migration shift assay shows the binding of hZαADAR1 to the intramolecular c-myc promoter G-quadruplex-forming DNA oligomer. To corroborate the binding of hZαADAR1 to the G-quadruplex, CD and NMR chemical shift perturbation analyses were conducted. CD results indicate that hZαADAR1 stabilizes the parallel-stranded conformation of the c-myc G-quadruplex. The NMR chemical shift perturbation data reveals that the G-quadruplex binding region in hZαADAR1 was almost identical to the Z-DNA binding region. 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