RNase P cleavage of pseudoknot substrates reveals differences in active site architecture that depend on residue N-1 in the 5’ leader

RNase P cleavage of pseudoknot substrates reveals differences in active site architecture that depend on residue N-1 in the 5’ leader

We show that a small biotin-binding RNA aptamer that folds into a pseudoknot structure acts as a substrate for bacterial RNase P RNA (RPR) with and without the RNase P C5 protein. Cleavage in the single-stranded region in loop 1 was shown to depend on the presence of a RCCA-motif at the 3’ end of th...

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Bibliographic Details
Main Authors: David M. Kosek, J. Luis Leal, Ema Kikovska-Stojanovska, Guanzhong Mao, Shiying Wu, Samuel C. Flores, Leif A. Kirsebom
Format: Article
Language:English
Published: Taylor & Francis Group 2025-12-01
Series:RNA Biology
Subjects:
RNase P
ribozyme
divalent metal ions
model substrates
tRNA processing
Online Access:https://www.tandfonline.com/doi/10.1080/15476286.2024.2427906
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https://www.tandfonline.com/doi/10.1080/15476286.2024.2427906

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