九州大学 研究者情報
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基本情報 研究活動 教育活動
寺本 岳大(てらもと たかまさ) データ更新日:2021.06.24

助教 /  農学研究院 生命機能科学部門 生物機能分子化学講座


主な研究テーマ
RNA結合タンパク質、硫酸転移酵素の構造生物学
キーワード:構造生物学、X線結晶構造解析
2020.02.
研究業績
主要原著論文
1. Teramoto T., b,Kaitany K.J., Kakuta Y., Kimura M., Fierke C.A., Hall T.M.T., Pentatricopeptide repeats of protein-only RNase P use a distinct mode to recognize conserved bases and structural elements of pre-tRNA, Nucleic Acids Research, 10.1093/nar/gkaa627, 2020.12, Pentatricopeptide repeat (PPR) motifs are α-helical structures known for their modular recognition of single-stranded RNA sequences with each motif in a tandem array binding to a single nucleotide. Protein-only RNase P 1 (PRORP1) in Arabidopsis thaliana is an endoribonuclease that uses its PPR domain to recognize precursor tRNAs (pre-tRNAs) as it catalyzes removal of the 5′-leader sequence from pre-tRNAs with its NYN metallonuclease domain. To gain insight into the mechanism by which PRORP1 recognizes tRNA, we determined a crystal structure of the PPR domain in complex with yeast tRNAPhe at 2.85 Å resolution. The PPR domain of PRORP1 bound to the structurally conserved elbow of tRNA and recognized conserved structural features of tRNAs using mechanisms that are different from the established single-stranded RNA recognition mode of PPR motifs. The PRORP1 PPR domain-tRNAPhe structure revealed a conformational change of the PPR domain upon tRNA binding and moreover demonstrated the need for pronounced overall flexibility in the PRORP1 enzyme conformation for substrate recognition and catalysis. The PRORP1 PPR motifs have evolved strategies for protein-tRNA interaction analogous to tRNA recognition by the RNA component of ribonucleoprotein RNase P and other catalytic RNAs, indicating convergence on a common solution for tRNA substrate recognition..
主要学会発表等
学会活動
所属学会名
生化学会

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