Proteome-wide capture of co-translational protein dynamics

2020 Fiscal Year Final Research Report

• Project/Area Number: 19K16044
• Research Category: Grant-in-Aid for Early-Career Scientists
• Allocation Type: Multi-year Fund
• Review Section: Basic Section 43010:Molecular biology-related
• Research Institution: Kyoto Sangyo University
• Principal Investigator: FUJIWARA Keigo 京都産業大学, タンパク質動態研究所, 研究員 (10814907)
• Project Period (FY): 2019-04-01 – 2021-03-31
• Keywords: 新生ポリペプチド鎖 / 翻訳アレスト / co-translational / リボソーム / TnDR法 / 枯草菌 / MifM

Outline of Final Research Achievements

There is no proteome-wide understanding of the extent to which nascent proteins progress to cotranslational maturation in the cell. In this study, we constructed and used an engineered transposon, TnDR, which carries translation arrest sequence of Bacillus subtilis MifM, to capture co-translational protein dynamic in the cell. We identified hundreds of proteins that cancel the elongation arrest, most probably reflecting their ability to initiate the maturation/localization process co-translationally. Case studies identify B. subtilis proteins that initiate assembly with a partner molecule before completion of translation. These results suggest that cotranslational maturation is a frequently occurring event in protein biogenesis.

Free Research Field

分子生物学

Academic Significance and Societal Importance of the Research Achievements

機能的なタンパク質に成熟化する機構の理解はタンパク質科学において重要である。本研究により、細胞内で実際に多くのタンパク質がco-translationalに局在化や複合体形成を起こし得ることがわかり、基礎生物学的に重要な知見が得られたと考えられる。また、TnDR法を用いて細胞内でおきるco-translationalなタンパク質動態を捉えることができた。この技術をより発展させることで、将来的にタンパク質科学において有用な技術になることが期待できる。