Human APNX protein is a dual function enzyme that have AP endnuclease activity and acethyltransferase activity.
| Project/Area Number |
26340020
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Risk sciences of radiation and chemicals
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| Research Institution | Tohoku University |
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Principal Investigator |
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | DNA修復酵素 / AP endonuclease / アセチル基転移酵素 / oxidative damage / PARP1 / acetyltransferase / DNA修復 / 酸化ストレス / アセチルトランスフェラーゼ |
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| Outline of Final Research Achievements |
The CYR motif was first identified in the human repair protein, PALF (ALPF), and found in various proteins of DNA metabolism, such as DNA repair and the DNA damage checkpoint. We found CG1218-PA and its human ortholog protein (APNX) that have CYR motif and DUF2228 domain, a domain of unknown function by searching database. We here analyzed the function of CG1218-PA in DNA damage response and found that CG1218-PA and its human ortholog APNX harboring DUF2228 are apurinic/apyrimidinic (AP) endonuclease. APNX interacts tightly with PARP1 and contributes to its activation after treatment of cells with alkylating agents. On the other hand, APNX have a partial similarity sequence of Tip60 and putative acetylCoA binding site. In vitro assay, APNX possess acethyltransferase activities against APNX itself and Tip60 protein. APNX plays an important role for the repair of DNA strand breaks and signaling of DNA damage in higher eukaryotic cells.
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Report
(4 results)
Research Products
(8 results)
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[Journal Article] The BRCA1/BARD1-interacting protein OLA1 functions in centrosome2014
Author(s)
Matsuzawa A, Kanno S, Nakayama M, Mochiduki H, Wei L, Shimaoka T, Furukawa Y, Kato K, Shibata S, Yasui A, Ishioka C, and Chiba N
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Journal Title
Molecular Cell
Volume: 53
Pages: 101-14
Related Report
Peer Reviewed / Open Access
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