2020 Fiscal Year Final Research Report
The physiological functions of protein arginine methylation.
| Project/Area Number |
17K01942
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biomolecular chemistry
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| Research Institution | University of Tsukuba |
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Principal Investigator |
KAKO Koichiro 筑波大学, 生命環境系, 講師 (60311594)
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| Project Period (FY) |
2017-04-01 – 2021-03-31
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| Keywords | アルギニンメチル化 / 線虫 / in vivo / LC-MS/MS |
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| Outline of Final Research Achievements |
We have already shown that both ADMA and SDMA are lost in mutant C. elegans lacking prmt-1, which is responsible for asymmetric dimethylation (ADMA) of protein arginine residues, and prmt-5, which is responsible for symmetric dimethylation (SDMA), but that monomethylarginine (MMA) is not completely lost in the prmt-1/prmt-5 double mutant.
In this study, we used reverse genetics and mass spectrometry techniques to search for methyltransferase genes that contribute to MMA conversion in vivo, and succeeded in obtaining mutants of the candidate genes.
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| Free Research Field |
生物有機化学、生化学
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| Academic Significance and Societal Importance of the Research Achievements |
メチル基転移酵素は、全ゲノムの約１％を占めるスーパーファミリーを形成するものの、基質が異なる酵素間では一次構造上の類似性がほとんど認められない。
本研究において、線虫や酵母など種の違いや基質の違いに捉われることなく、広く既知のメチル基転移酵素に認められる二次構造上の類似性に基づいて、新規のメチル化酵素を探索し得られた知見は、単に線形動物のタンパク質アルギニンメチル化に留まらず、より高等な哺乳動物における様々な基質に対するメチル化酵素の研究にも、十分活用できると考えられる。
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