2011 Fiscal Year Final Research Report
Analysis of nuclear lipidation in gene regulation
| Project/Area Number |
22780086
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied biochemistry
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| Research Institution | The University of Tokyo |
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Principal Investigator |
YOKOYAMA Atsushi 東京大学, 分子細胞生物学研究所, 特任助教 (20572332)
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| Project Period (FY) |
2010 – 2011
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| Keywords | 遺伝子発現 / 翻訳後修飾 |
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| Research Abstract |
This year we performed proteomic analysis of purified endogenous HN4 protein using the scheme established last year.
First of all, we purified endogenous HNF4 protein by affinity purification, then samples were subjected to LC-MS/MS analysis. From this experiment, we identified 14 PTM sites in HNF4 protein such as phosphorylation, acetylation, methylation and ubiquitilation. This result was reported to the scientific journal as an original paper(Yokoyama et al., Biochem Biophys Res Commun, 2011, 410(4): 749-5). However, we could not identify the lipidation of HNF4 in this experiment.
Furthermore, we adopted the novel method "click-it reaction" for the proteomic analysis of nuclear lipidation. In this method, labeled proteins were purified by avidin beads, and then subjected to the LC-MS/MS analysis. As a result, we identified various proteins including HNF4 and histone protein. We think this result implies that nuclear lipidation has more global role than we expected before, and now we are preparing the manuscript for the paper concerning this results.
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Research Products
(9 results)
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[Journal Article] O-GlcNAcylation of histone H2B facilitates its monoubiquitination2011
Author(s)
Fujiki R, Hashiba W, Sekine H, Yokoyama A, Chikanishi T, Ito S, Imai Y, Ohtake F, Kitagawa H, Kim J, Roeder RG, He HH, Brown M and Kato S
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Journal Title
Nature
Volume: vol.480, No.7378
Pages: 557-560
Peer Reviewed
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