Analysis of proteins involved in the MAT2A mRNA stability control
Project/Area Number |
17K07278
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Molecular biology
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Research Institution | Tohoku University |
Principal Investigator |
Shima Hiroki 東北大学, 医学系研究科, 助手 (00448268)
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Project Period (FY) |
2017-04-01 – 2020-03-31
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Project Status |
Completed (Fiscal Year 2019)
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Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2019: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2018: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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Keywords | RNA / S-アデノシルメチオニン / N6-メチルアデノシン / 転写後調節 / RNA安定性 / RNA結合タンパク質 / 発現制御 |
Outline of Final Research Achievements |
The expression of MAT2A, the ubiquitous S-adenosylmethionine (SAM) synthetase in mammals, is regulated in a intracellular SAM-responsive manner. The feedback control is mediated by methyl-6-adenosine (m6A) modification occurring six specific adenosine residues in the hairpins located in the 3' UTR of the MAT2A mRNA. The research aimed at identification of RNA binding proteins interacting with the MAT2A 3'UTR. By comparing associating proteins between WT and m6A-site-mutant 3'UTR, we found RNA-binding proteins involved in the stability control of the MAT2A mRNA.
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Academic Significance and Societal Importance of the Research Achievements |
mRNAの転写後調節は、遺伝子発現制御の主要な仕組みの一つである。m6A修飾はmRNAに見られる修飾のうち最も多いものであり、これによるRNA制御の分子メカニズムは近年の注目を集めている。本研究の結果はMAT2A mRNAを対象としてとりあげ、m6AによるRNA制御のメカニズムの理解に資するものであるとともに、m6A 制御や細胞内SAM 量調節の異常を原因とする疾患の研究のための基礎的な情報としても貢献できる可能性もある。
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Report
(4 results)
Research Products
(12 results)
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[Journal Article] Zinc finger-IRF composite elements bound by Ikaros/IRF4 complexes function as gene repression in plasma cell2018
Author(s)
Kyoko Ochiai, Haruka Kondo, Yasunobu Okamura, Hiroki Shima, Yuko Kurokochi, Kazumi Kimura, Ryo Funayama, Takeshi Nagashima, Keiko Nakayama, Katsuyuki Yui, Kengo Kinoshita and Kazuhiko Igarashi
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Journal Title
Blood advances
Volume: Apr 24;2(8)
Issue: 8
Pages: 883-894
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] Phosphorylation of BACH1 switches its function from transcription factor to mitotic chromosome regulator and promotes its interaction with HMMR.2018
Author(s)
Li J, Shima H, Nishizawa H, Ikeda M, Brydun A, Matsumoto M, Kato H, Saiki Y, Liu L, Watanabe-Matsui M, Iemura K, Tanaka K, Shiraki T, Igarashi K.
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Journal Title
Biochemical Journal
Volume: 475
Issue: 5
Pages: 981-1002
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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