Constructing an RNA self-replication system through peptide structuring

2023 Fiscal Year Final Research Report

• Project/Area Number: 20K14599
• Research Category: Grant-in-Aid for Early-Career Scientists
• Allocation Type: Multi-year Fund
• Review Section: Basic Section 17050:Biogeosciences-related
• Research Institution: Institute of Physical and Chemical Research
• Principal Investigator: Li Peiying 国立研究開発法人理化学研究所, 生命機能科学研究センター, 研究員 (00862062)
• Project Period (FY): 2020-04-01 – 2024-03-31
• Keywords: 生命の起源 / リボザイム / ペプチド / 自己集合

Outline of Final Research Achievements

In this study, we investigated the effects of simple peptides capable of forming aggregate structures via self-assembly on ribozyme activity, with the aim of understanding the co-evolution between RNA and peptide on early earth. As a result, we found that simple cationic peptides with hydrophobic domain can self-assemble and form solid aggregates containing amyloid structures. These aggregates can concentrate RNAs on their surface and enhance the activity of bound ribozymes. Furthermore, we found that the ribozyme activity is affected by the sequence of the self-assembling peptide and salt concentration. Such simple peptides may have played a beneficial role in supporting ribozymes under conditions with various salt concentrations on early earth.

Free Research Field

合成生物学

Academic Significance and Societal Importance of the Research Achievements

現代の生命では核酸やタンパク質を含む多くの分子種が協調してそのシステムを構築しているが，そのような複雑な系が如何に誕生し，進化してきたのかは生命を理解するための本質な問いである．本研究では複数分子種が存在する環境下でのRNA自己複製の実現に向けて，単純なペプチドの構造化とその機能に着目し，RNAとの共存の際にリボザイム活性にどのような影響を与えるかを明らかにした．本研究では，核酸結合性のペプチドが自己集合して構造化することが生命誕生に必須であった可能性を示し，そこからさらにより複雑な構造・機能をもったタンパク質が進化してきたことの説明にもつながる．