| Project/Area Number |
11470037
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General medical chemistry
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| Research Institution | RIKEN |
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Principal Investigator |
YOKOYAMA Kazunari k. RIKEN, Gene Engineering Division, Head, 遺伝子材料開発室, 室長(副主任研究員待遇) (80182707)
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| Co-Investigator(Kenkyū-buntansha) |
TSUTSUI Hatsumi RIKEN, Experimental Animal Division, Technical researcher, 遺伝子材料開発室, 技師(研究職) (00301763)
MURATA Takehide RIKEN, Gene Engineering Division, Senior Researcher, 遺伝子材料開発室, 先任研究員 (50281621)
SARAI Akinori RIKEN, Mol. Genetics, Vice-Chief researcher, 分子遺伝学研究室, 副主任研究員 (20221286)
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| Project Period (FY) |
1999 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥12,400,000 (Direct Cost: ¥12,400,000)
Fiscal Year 2001: ¥2,500,000 (Direct Cost: ¥2,500,000)
Fiscal Year 2000: ¥2,800,000 (Direct Cost: ¥2,800,000)
Fiscal Year 1999: ¥7,100,000 (Direct Cost: ¥7,100,000)
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| Keywords | MAZ / p300 / Triplex / Acetylation / Deacetylation / GC rich element / Histone / Zinc finger / c-mycプロモーター / 三重鎖結合因子 / コアクチベクター / HAT活性 / クロマチン / SP1ファミリー / ヒストン脱アセチル化 / コアクチベーター / 相互作用 / c-mysプロモーター / リン酸化反応 |
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| Research Abstract |
The control of gene expression by antigene oligonucleotides rests upon the specific recognition of double-helical DNA by triplex-forming oligonucleotides. The development of the antigene strategy requires access to the targeted DNA sequence within the chromatin structure of the cell nucleus. In this study we isolated MAZ (Myc associated zinc finger protein) gene and characterized its function for the chromatin remodeling. The promoter region of MAZ gene is composed of G and C (G+C content 88.4%). The gene for MAZ was mapped to chromosome 16p11.2 by fluorescence in situ hybridization (FISH). The entire exon-intron structure of the human gene for MAZ is approximately 6.0 kb long. It includes promoter, five exons, four introns and a 3'-untranslated region. MAZ and Sp1 interact with the same GC-rich DNA-binding sites apparently sharing DNA-binding sites with each other and both factors regulated the expression of the housekeeping gene, MAZ, negatively. The zinc fingers of F2 and F3 for Spl showed the same structure as those of F4 and F3 for MAAZ, respectively. Both are interchangeable. We also identified the phosphorylation site of MAZ, serine residue at position 480 by cretation kinase II. We also showed the MAZ associated molecule is DCC tumor suppressor protein and their interaction is required for the terminal differentiation of P19 cells in response to RA. The transcritional coactivator p300 is also associated with MAZ to regulate its transcription. The precise map of p300 associated with MAZ is necessary for understanding the network of signals of transcriptional factor MAZ for chromatin remodeling.
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