Substrate Recognition by Human RNase P: Identification of Small, Model Substrates for the Enzyme

Overview

Journal EMBO J

Specialties Biotechnology
Molecular Biology

Date 1995 Jan 3

PMID 7828588

Citations 36

Authors

Y Yuan

S Altman

Affiliations

Soon will be listed here.

Abstract

RNase P from HeLa cells can efficiently cleave tRNA precursor molecules in vitro but cannot cleave potential substrates from which the D, anticodon and variable loops and stems of the tRNA moiety have all been removed. However, molecules from which the latter subdomains have been removed individually do serve as substrates. We show here that molecules that contain only a 5' leader sequence, the acceptor stem and the T stem and loop of the tRNA domain, and a bulge as small as one nucleotide downstream from nucleotide 7 in the tRNA sequence at the junction of the two stems, can serve as substrates for human RNase P. The identity of the nucleotide in the bulge is important in determining both the efficiency of the cleavage and the conformation of the substrate and/or the enzyme-substrate complex. We also show that the human enzyme locates the appropriate site for cleavage of its substrates in part by 'measuring' the length of the helices in the acceptor and T stems in both model and natural substrates.

Citing Articles

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Liu Y, He S, Pyo A, Zheng S, Chen M, Cheloufi S bioRxiv. 2025; .

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Structural basis of MALAT1 RNA maturation and mascRNA biogenesis.

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Discovery, structure, mechanisms, and evolution of protein-only RNase P enzymes.

Rossmanith W, Giege P, Hartmann R J Biol Chem. 2024; 300(3):105731.

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Synthetic riboswitches for the analysis of tRNA processing by eukaryotic RNase P enzymes.

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