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Structural insight into precursor tRNA processing by yeast ribonuclease P.

Authors :
Pengfei Lan
Ming Tan
Yuebin Zhang
Shuangshuang Niu
Juan Chen
Shaohua Shi
Shuwan Qiu
Xuejuan Wang
Xiangda Peng
Gang Cai
Hong Cheng
Jian Wu
Guohui Li
Ming Lei
Source :
Science. 11/9/2018, Vol. 362 Issue 6415, p657-657. 1p. 1 Diagram.
Publication Year :
2018

Abstract

The article focuses on a study according to which all Ribonuclease P (RNase P) ribozymes share a substrateinduced catalytic mechanism of pre-RNA processing. It mentions that RNase P is a ribonucleoprotein complex, composed of a single catalytic RNA components. It states that the Rpr1 RNA adopts an extended single-layered conformation that maintains a central helical core but lacks longrange RNA-RNA interactions that are essential for structural stability in bacterial RNase P.

Details

Language :
English
ISSN :
00368075
Volume :
362
Issue :
6415
Database :
Academic Search Index
Journal :
Science
Publication Type :
Academic Journal
Accession number :
132986555
Full Text :
https://doi.org/10.1126/science.aat6678