Elucidation of dynamic-molecular recognition mechanism by the dimeric RNA maturation enzymes

2017 Fiscal Year Final Research Report

• Project/Area Number: 15K06975
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Structural biochemistry
• Research Institution: Ehime University
• Principal Investigator: Hirata Akira 愛媛大学, 理工学研究科(工学系), 講師 (60527381)
• Project Period (FY): 2015-04-01 – 2018-03-31
• Keywords: tRNA maturation / tRNA modification / recognition mechanism / X-ray structure / SAXS analysis / tRNA methyltransferase / RNA splicing

Outline of Final Research Achievements

The X-ray structure of archaeal aTrm11, which is homologous to the catalytic unit of Trm11 in eukaryotic tRNA (m2G10) methyltransferase Trm11-Trm112, is determined, and the structure-guided biochemical analysis provides mechanistic insight into site specificity of archaeal Trm11 and furher proposes a molecular ruler mechanism by which the Trm11 defines the distance and angle from the end of 3'-CCA in substrate tRNA to methylation site. The structural and functional analyses of RNA-splicing endonuclease (EndA) from hyperthermophilic archaeon Methanopyrus kandleri have demonstrated that the MKA EndA consists of heterodimer （αβ)2 and shows a constrain substrate specificity.

Free Research Field

構造生物化学