Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme

Ribonulease P is a conserved ribozyme present in all kingdoms of life that is involved in the 5′ maturation step of tRNAs. Here the authors determine the structure of an archaeal RNase P holoenzyme that reveals how archaeal RNase P recognizes its tRNA substrate and suggest a conserved catalytic mech...

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Autores principales:	Futang Wan, Qianmin Wang, Jing Tan, Ming Tan, Juan Chen, Shaohua Shi, Pengfei Lan, Jian Wu, Ming Lei
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/990f5b49fd464df0a00d10cd45aaf44c
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spelling	oai:doaj.org-article:990f5b49fd464df0a00d10cd45aaf44c2021-12-02T16:57:35ZCryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme10.1038/s41467-019-10496-32041-1723https://doaj.org/article/990f5b49fd464df0a00d10cd45aaf44c2019-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10496-3https://doaj.org/toc/2041-1723Ribonulease P is a conserved ribozyme present in all kingdoms of life that is involved in the 5′ maturation step of tRNAs. Here the authors determine the structure of an archaeal RNase P holoenzyme that reveals how archaeal RNase P recognizes its tRNA substrate and suggest a conserved catalytic mechanism amongst RNase Ps despite structural variability.Futang WanQianmin WangJing TanMing TanJuan ChenShaohua ShiPengfei LanJian WuMing LeiNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Futang Wan Qianmin Wang Jing Tan Ming Tan Juan Chen Shaohua Shi Pengfei Lan Jian Wu Ming Lei Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme
description	Ribonulease P is a conserved ribozyme present in all kingdoms of life that is involved in the 5′ maturation step of tRNAs. Here the authors determine the structure of an archaeal RNase P holoenzyme that reveals how archaeal RNase P recognizes its tRNA substrate and suggest a conserved catalytic mechanism amongst RNase Ps despite structural variability.
format	article
author	Futang Wan Qianmin Wang Jing Tan Ming Tan Juan Chen Shaohua Shi Pengfei Lan Jian Wu Ming Lei
author_facet	Futang Wan Qianmin Wang Jing Tan Ming Tan Juan Chen Shaohua Shi Pengfei Lan Jian Wu Ming Lei
author_sort	Futang Wan
title	Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme
title_short	Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme
title_full	Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme
title_fullStr	Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme
title_full_unstemmed	Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme
title_sort	cryo-electron microscopy structure of an archaeal ribonuclease p holoenzyme
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/990f5b49fd464df0a00d10cd45aaf44c
work_keys_str_mv	AT futangwan cryoelectronmicroscopystructureofanarchaealribonucleasepholoenzyme AT qianminwang cryoelectronmicroscopystructureofanarchaealribonucleasepholoenzyme AT jingtan cryoelectronmicroscopystructureofanarchaealribonucleasepholoenzyme AT mingtan cryoelectronmicroscopystructureofanarchaealribonucleasepholoenzyme AT juanchen cryoelectronmicroscopystructureofanarchaealribonucleasepholoenzyme AT shaohuashi cryoelectronmicroscopystructureofanarchaealribonucleasepholoenzyme AT pengfeilan cryoelectronmicroscopystructureofanarchaealribonucleasepholoenzyme AT jianwu cryoelectronmicroscopystructureofanarchaealribonucleasepholoenzyme AT minglei cryoelectronmicroscopystructureofanarchaealribonucleasepholoenzyme
_version_	1718382516376698880

Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme

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