Structural and functional analyses for the novel restriction enzyme R.PabI and its homologues in pathogenic bacteria.
| Project/Area Number |
26712012
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| Research Category |
Grant-in-Aid for Young Scientists (A)
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| Allocation Type | Partial Multi-year Fund |
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| Research Field |
Applied biochemistry
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| Research Institution | The University of Tokyo |
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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 |
¥24,180,000 (Direct Cost: ¥18,600,000、Indirect Cost: ¥5,580,000)
Fiscal Year 2016: ¥7,410,000 (Direct Cost: ¥5,700,000、Indirect Cost: ¥1,710,000)
Fiscal Year 2015: ¥7,540,000 (Direct Cost: ¥5,800,000、Indirect Cost: ¥1,740,000)
Fiscal Year 2014: ¥9,230,000 (Direct Cost: ¥7,100,000、Indirect Cost: ¥2,130,000)
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| Keywords | 制限酵素 / タンパク質 / 結晶構造解析 / DNAグリコシラーゼ / 構造解析 / 蛋白質 / 核酸 / 酵素 / 抗生物質 / X線結晶構造解析 |
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| Outline of Final Research Achievements |
In this study, we analyzed the structure and function of the half pipe superfamily restriction enzyme, which is conserved in pathogenic bacteria such as Helicobacter and Campylobacter and in some hyperthermophilic archaea. The crystal structures of R.PabI, which is the first half pipe superfamily restriction enzyme found in the hyperthermophilic archaea Pyrococcus abyssi, in complexes with substrate, product, and nonspecific DNAs showed that R.PabI cleaves not a phosphodiester bond but an N-glycosidic bond in DNA, indicating that R.PabI cleaves DNA using DNA glycosylase activity. This is the first example of restriction enzymes that functions by using other than endonuclease activity (restriction DNA glycosylase). We also determined the crystal structures of half pipe super family restriction enzymes from pathogenic bacteria.
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Report
(4 results)
Research Products
(9 results)
