2013 Fiscal Year Final Research Report
A novel method to identify nuclear proteins modified with N-acetylglucosamine by using a soluble glycosyltransferase having nuclear-localization signal
| Project/Area Number |
24659026
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Single-year Grants |
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| Research Field |
Biological pharmacy
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| Research Institution | The University of Tokyo |
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Principal Investigator |
YAMAMOTO Kazuo 東京大学, 新領域創成科学研究科, 教授 (20174782)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Keywords | 生化学 / 糖鎖 / 翻訳後修飾 / 核内タンパク質 |
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| Research Abstract |
Glycosylation of proteins occurs in the lumens of the endoplasmic reticulum and the Golgi apparatus, which resulted in diverse structures of carbohydrate moieties. By contrast, addition of N-acetylglucosamine (GlcNAc) to serine and threonine is a unique glycosylation reaction occurred in nucleus and cytoplasm. We expressed a soluble glycosyltransferase having nuclear-localization signal in the cell and induced further elongation of GlcNAc residue. By using lectin affinity chromatography and mass spectrometry, we comprehensively identified O-GlcNAc modified proteins and their GlcNAc-modified amino acid residues.
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