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![Novel interaction of the z-dna binding domain of human ADAR1 with the oncogenic c-Myc promoter g-quadruplex. [link]](https://bibbase.org/img/filetypes/link.svg "link")
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},
}
Downloads: 0
{"_id":"P3FwqQZKoqADKZPRQ","bibbaseid":"kang-le-kim-hur-kim-park-novelinteractionofthezdnabindingdomainofhumanadar1withtheoncogeniccmycpromotergquadruplex-2014","author_short":["Kang, H.","Le, T. V. T.","Kim, K.","Hur, J.","Kim, K. K.","Park, H."],"bibdata":{"bibtype":"article","type":"article","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":[{"propositions":[],"lastnames":["Kang"],"firstnames":["Hyun-Jin"],"suffixes":[]},{"propositions":[],"lastnames":["Le"],"firstnames":["Tuong","Vy","Thi"],"suffixes":[]},{"propositions":[],"lastnames":["Kim"],"firstnames":["Kyungmin"],"suffixes":[]},{"propositions":[],"lastnames":["Hur"],"firstnames":["Jeonghwan"],"suffixes":[]},{"propositions":[],"lastnames":["Kim"],"firstnames":["Kyeong","Kyu"],"suffixes":[]},{"propositions":[],"lastnames":["Park"],"firstnames":["Hyun-Ju"],"suffixes":[]}],"year":"2014","pmid":"24813121","note":"Publisher: Elsevier Ltd","keywords":"#nosource, Z-DNA binding domain of human ADAR1, c-Myc G-Quadruplex","pages":"2594–2604","bibtex":"@article{Kang2014,\n\ttitle = {Novel interaction of the z-dna binding domain of human {ADAR1} with the oncogenic c-{Myc} promoter g-quadruplex.},\n\tvolume = {426},\n\tissn = {1089-8638},\n\turl = {http://www.sciencedirect.com/science/article/pii/S0022283614002289},\n\tdoi = {10.1016/j.jmb.2014.05.001},\n\tabstract = {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.},\n\tnumber = {14},\n\tjournal = {Journal of molecular biology},\n\tauthor = {Kang, Hyun-Jin and Le, Tuong Vy Thi and Kim, Kyungmin and Hur, Jeonghwan and Kim, Kyeong Kyu and Park, Hyun-Ju},\n\tyear = {2014},\n\tpmid = {24813121},\n\tnote = {Publisher: Elsevier Ltd},\n\tkeywords = {\\#nosource, Z-DNA binding domain of human ADAR1, c-Myc G-Quadruplex},\n\tpages = {2594--2604},\n}\n\n","author_short":["Kang, H.","Le, T. V. T.","Kim, K.","Hur, J.","Kim, K. K.","Park, H."],"key":"Kang2014-1","id":"Kang2014-1","bibbaseid":"kang-le-kim-hur-kim-park-novelinteractionofthezdnabindingdomainofhumanadar1withtheoncogeniccmycpromotergquadruplex-2014","role":"author","urls":{"Paper":"http://www.sciencedirect.com/science/article/pii/S0022283614002289"},"keyword":["#nosource","Z-DNA binding domain of human ADAR1","c-Myc G-Quadruplex"],"metadata":{"authorlinks":{}},"html":""},"bibtype":"article","biburl":"https://bibbase.org/zotero/eric.larG4","dataSources":["4i5C7S78DvJNsaHyg","5L2zM5wNE5CBYNuea"],"keywords":["#nosource","z-dna binding domain of human adar1","c-myc g-quadruplex"],"search_terms":["novel","interaction","dna","binding","domain","human","adar1","oncogenic","myc","promoter","quadruplex","kang","le","kim","hur","kim","park"],"title":"Novel interaction of the z-dna binding domain of human ADAR1 with the oncogenic c-Myc promoter g-quadruplex.","year":2014}