A novel method to identify nuclear proteins modified with N-acetylglucosamine by using a soluble glycosyltransferase having nuclear-localization signal
| Project/Area Number |
24659026
|
|---|
| Research Category |
Grant-in-Aid for Challenging Exploratory Research
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
Biological pharmacy
|
|---|
| Research Institution | The University of Tokyo |
|---|
Principal Investigator |
YAMAMOTO Kazuo 東京大学, 新領域創成科学研究科, 教授 (20174782)
|
|---|
| Project Period (FY) |
2012-04-01 – 2014-03-31
|
| Project Status |
Completed (Fiscal Year 2013)
|
| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2013: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2012: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
|---|
| Keywords | 生化学 / 糖鎖 / 翻訳後修飾 / 核内タンパク質 |
|---|
| 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.
|
Report
(3 results)
Research Products
(3 results)
