2016 Fiscal Year Final Research Report
Devolopment of a novel method to identify E3 ligase substrates
| Project/Area Number |
15K15058
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
General medical chemistry
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| Research Institution | Hokkaido University |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Keywords | ユビキチン / ユビキチンリガーゼ |
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| Outline of Final Research Achievements |
Since ubiquitin ligase (E3) has the substrate specificity of ubiquitination, identifications of specific substrates of each E3 enzymes and of their ubiquitination sites are important for understanding various biological phenomena. In recent years, Toczyski and colleagues have proposed a ligase trap method using a fusion probe of an ubiquitin-binding domain (UBA) and an E3, and Yoshida and colleagues have proposed a TR-TUBE method combining Tandem Ubiquitin Binding Entity (TUBE) and K-εGG-specific antibody. We attempted to develop a more advanced substrate identification method by adding some improvements in their methods and succeeded in improving the sensitivity. By using this method, it is expected that the functional analysis of E3 would be accelerated.
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| Free Research Field |
医化学一般
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