Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme

Futang Wan, Qianmin Wang, Jing Tan, Ming Tan, Juan Chen, Shaohua Shi, Pengfei Lan (), Jian Wu () and Ming Lei ()
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Futang Wan: Chinese Academy of Sciences
Qianmin Wang: Shanghai Jiao Tong University School of Medicine
Jing Tan: Chinese Academy of Sciences
Ming Tan: Chinese Academy of Sciences
Juan Chen: Shanghai Jiao Tong University School of Medicine
Shaohua Shi: Shanghai Jiao Tong University School of Medicine
Pengfei Lan: Shanghai Jiao Tong University School of Medicine
Jian Wu: Shanghai Jiao Tong University School of Medicine
Ming Lei: Shanghai Jiao Tong University School of Medicine

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: Abstract Ribonuclease P (RNase P) is an essential ribozyme responsible for tRNA 5′ maturation. Here we report the cryo-EM structures of Methanocaldococcus jannaschii (Mja) RNase P holoenzyme alone and in complex with a tRNA substrate at resolutions of 4.6 Å and 4.3 Å, respectively. The structures reveal that the subunits of MjaRNase P are strung together to organize the holoenzyme in a dimeric conformation required for efficient catalysis. The structures also show that archaeal RNase P is a functional chimera of bacterial and eukaryal RNase Ps that possesses bacterial-like two RNA-based anchors and a eukaryal-like protein-aided stabilization mechanism. The 3′-RCCA sequence of tRNA, which is a key recognition element for bacterial RNase P, is dispensable for tRNA recognition by MjaRNase P. The overall organization of MjaRNase P, particularly within the active site, is similar to those of bacterial and eukaryal RNase Ps, suggesting a universal catalytic mechanism for all RNase Ps.

Date: 2019
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DOI: 10.1038/s41467-019-10496-3

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