Identification of target genes of transcription elongation factor Elongin A and analysis of its regulation
Project/Area Number |
15K08177
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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 |
General physiology
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Research Institution | Kochi University |
Principal Investigator |
Yasukawa Takashi 高知大学, 教育研究部医療学系基礎医学部門, 助教 (60291936)
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Research Collaborator |
TSUTSUI Aya
|
Project Period (FY) |
2015-10-21 – 2018-03-31
|
Project Status |
Completed (Fiscal Year 2017)
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Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2017: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2016: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2015: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
|
Keywords | Elongin A / 転写伸長因子 / 神経分化 / ユビキチンリガーゼ |
Outline of Final Research Achievements |
The possibility that homeobox (Hox) genes and non-coding RNA (Miat) gene were the target genes of Elongin A (EloA) was suggested by ChIP-Seq analysis using anti-RNA polymerase II (Pol II) and anti-EloA antibodies. These genes play an important role of the neural development. Moreover, we demonstrated (i) that assembly of the EloA ubiquitin ligase (EloA-E3) is triggered following DNA damage as well as by treatment of cells with drugs that block Pol II elongation (ii) that the assembly is also triggered by induction of ER and nutrient stress and by retinoic acid treatment (iii) that EloA-E3 associate in cells with the Cockayne syndrome B (CSB) protein and (iv) that this interaction is also induced by DNA-damaging agents and alpha-amanitin (v) CSB protein promotes stable recruitment of the EloA-E3 to sites of DNA damage.
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Report
(4 results)
Research Products
(2 results)
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[Journal Article] Cockayne syndrome B protein regulates recruitment of the Elongin A ubiquitin ligase to sites of DNA damage.2017
Author(s)
Weems JC, Slaughter BD, Unruh JR, Boeing S, Hall SM, McLaird MB, Yasukawa T, Aso T, Svejstrup JQ, Conaway JW, Conaway RC
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Journal Title
J. Biol. Chem.
Volume: 292
Issue: 16
Pages: 6431-6437
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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