2011 Fiscal Year Final Research Report
Analysis of regulatory mechanisms of Protein L-isoaspartyl(D-aspartyl) O-methyltransferase(PIMT) gene expression.
| Project/Area Number |
21590069
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biological pharmacy
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| Research Institution | Kitasato University |
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Principal Investigator |
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| Project Period (FY) |
2009 – 2011
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| Keywords | 分子生物学 |
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| Research Abstract |
In order to clarify the transcriptional regulatory mechanisms of PIMT, isomerized protein repair enzyme, we cloned and functionally characterized the 5'-flanking(promoter) region of the gene. The putative promoter activity was confirmed using dual luciferase reporter gene assay system. The minimal region required for basal activity of the promoter was determined by generating a series of deletion and point mutation constructs. The binding protein(s) to the minimal region was briefly purified using biotin-labeled DNA probe, and subsequently LC-MS/MS analysis was performed and a transcriptional factor, NRF1, was identified. Binding activity of NRF1 to the minimal region was confirmed using electrophoretic mobility shift assay and chromatin immunoprecipitation assay.
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[Journal Article] Spatiotemporal localization of D-amino acid oxidase and D-aspartate oxidases during development in Caenorhabditis elegans2012
Author(s)
Saitoh Y, Katane M, Kawata T, Maeda K, Sekine M, Furuchi T, Kobuna H, Sakamoto T, Inoue T, Arai H, Nakagawa Y, Homma H
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Journal Title
Mol Cell Biol
Volume: 32(10)
Pages: 1967-1983
DOI
Peer Reviewed
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