Minimal protein-only RNase P structure reveals insights into tRNA precursor recognition and catalysis
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ABSTRACT:
SUBMITTER: Naruhiko Adachi
PROVIDER: EMPIAR-11072 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Minimal protein-only RNase P structure reveals insights into tRNA precursor recognition and catalysis.
Teramoto Takamasa T Koyasu Takeshi T Adachi Naruhiko N Kawasaki Masato M Moriya Toshio T Numata Tomoyuki T Senda Toshiya T Kakuta Yoshimitsu Y
The Journal of biological chemistry 20210731 3
Ribonuclease P (RNase P) is an endoribonuclease that catalyzes the processing of the 5' leader sequence of precursor tRNA (pre-tRNA). Ribonucleoprotein RNase P and protein-only RNase P (PRORP) in eukaryotes have been extensively studied, but the mechanism by which a prokaryotic nuclease recognizes and cleaves pre-tRNA is unclear. To gain insights into this mechanism, we studied homologs of Aquifex RNase P (HARPs), thought to be enzymes of approximately 23 kDa comprising only this nuclease domain ...[more]
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