2025-07-04 九州大学
図1. HARP12量体(レインボーカラー)とtRNA前駆体(灰色:5分子)複合体の立体構造 (左)上から見た図 (右)側面から見た図
<関連情報>
- https://www.kyushu-u.ac.jp/ja/researches/view/1284
- https://www.kyushu-u.ac.jp/f/62314/25_0704_02.pdf
- https://www.nature.com/articles/s41467-025-60002-1
細菌の最小RNase Pによる転移RNAプロセシングの構造基盤 Structural basis of transfer RNA processing by bacterial minimal RNase P
Takamasa Teramoto,Takeshi Koyasu,Takashi Yokogawa,Naruhiko Adachi,Kouta Mayanagi,Takahiro Nakamura,Toshiya Senda & Yoshimitsu Kakuta
Nature Communications Published:01 July 2025
DOI:https://doi.org/10.1038/s41467-025-60002-1
Abstract
Precursor tRNAs (pre-tRNAs) require nucleolytic removal of 5′-leader and 3′-trailer sequences for maturation, which is essential for proper tRNA function. The endoribonuclease RNase P exists in diverse forms, including RNA- and protein-based RNase P, and removes 5′-leader sequences from pre-tRNAs. Some bacteria and archaea possess a unique minimal protein-based RNase P enzyme, HARP, which forms dodecamers with twelve active sites. Here, we present cryogenic electron microscopy structures of HARP dodecamers complexed with five pre-tRNAs, and we show that HARP oligomerization enables specific recognition of the invariant distance between the acceptor stem 5′-end and the TψC-loop, functioning as a molecular ruler—a feature representing convergent evolution among RNase P enzymes. The HARP dodecamer uses only five active sites for 5′-leader cleavage, while we identify a 3′-trailer cleavage activity in the remaining seven sites. This elucidation reveals how small proteins evolve through oligomerization to adapt a pivotal biological function (5′-leader processing) and acquire a novel function (3′-trailer processing).
