2022 Fiscal Year Final Research Report
Identification of a new ubiquitin proteoform
Project/Area Number |
20K21408
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Research Category |
Grant-in-Aid for Challenging Research (Exploratory)
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Allocation Type | Multi-year Fund |
Review Section |
Medium-sized Section 43:Biology at molecular to cellular levels, and related fields
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Research Institution | Hoshi University |
Principal Investigator |
Ohtake Fumiaki 星薬科大学, 先端生命科学研究所, 特任准教授 (60447373)
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Project Period (FY) |
2020-07-30 – 2023-03-31
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Keywords | ユビキチン / プロテアソーム / プロテオミクス / 翻訳後修飾 |
Outline of Final Research Achievements |
Ubiquitin is a small protein consisting of 76 amino acids and serve as a source of a post-translational modification called ubiquitylation. Ubiquitylation regulates function or destiny of substrate proteins, yet, the diversity of the role of ubiquitin is not fully understood. In this study, we established the top-down and middle-down mass spectrometry for ubiquitin. Subsequently, we found that the cleaved ubiquitin, lacking the C-terminal double glycines, is accumulated after proteasomal inhibition. Moreover, the C-terminally cleaved ubiquitin interacts with specific binding proteins in vitro.
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Free Research Field |
分子生物学
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Academic Significance and Societal Importance of the Research Achievements |
ユビキチン・プロテアソーム系は細胞内の主要なタンパク質分解システムの一つであり、その破綻はがんや神経変性疾患、炎症性疾患など、様々な疾病につながることが知られている。そのため、本研究で見出したユビキチンの質量分析手法や新たなユビキチンのプロテオフォームは、将来的にユビキチン系のさらなる理解に貢献し、ユビキチン系に基づいた疾患に対する治療法開発の一助となることが期待される。
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