Go to page

Bibliographic Metadata

Substrate recognition and cleavage-site selection by a single-subunit protein-only RNase P
AuthorRossmanith, Walter ; Hartmann, Roland K. ; Toth, Ursula ; Lindenhofer, Dominik ; Goessringer, Markus ; Brillante, Nadia
Published in
Nucleic Acids Research, Oxford, 2016, Vol. 44, Issue 5, page 2323-2336
PublishedOxford : Oxford University Press, 2016
Document typeJournal Article
Keywords (EN)precursor-transfer-rna / bacterial ribonuclease p / bacillus-subtilis / escherichia-coli / mediated cleavage / 5' leader / catalytic strategies / processing enzyme / metal-ions / binding
Project-/ReportnumberI 299-B12
URNurn:nbn:at:at-ubmuw:3-1308 Persistent Identifier (URN)
 The work is publicly available
Substrate recognition and cleavage-site selection by a single-subunit protein-only RNase P [1.73 mb]
Abstract (English)

RNase P is the enzyme that removes 5' extensions from tRNA precursors. With its diversity of enzyme forms-either protein- or RNA-based, ranging from single polypeptides to multi-subunit ribonucleoproteins-the RNase P enzyme family represents a unique model system to compare the evolution of enzymatic mechanisms. Here we present a comprehensive study of substrate recognition and cleavage-site selection by the nuclear single-subunit proteinaceous RNase P PRORP3 from Arabidopsis thaliana. Compared to bacterial RNase P, the best-characterized RNA-based enzyme form, PRORP3 requires a larger part of intact tRNA structure, but little to no determinants at the cleavage site or interactions with the 5' or 3' extensions of the tRNA. The cleavage site depends on the combined dimensions of acceptor stem and T domain, but also requires the leader to be single-stranded. Overall, the single-subunit PRORP appears mechanistically more similar to the complex nuclear ribonucleoprotein enzymes than to the simpler bacterial RNase P. Mechanistic similarity or dissimilarity among different forms of RNase P thus apparently do not necessarily reflect molecular composition or evolutionary relationship.

The PDF-Document has been downloaded 3 times.
CC-BY-NC-License (4.0)Creative Commons Attribution - NonCommercial 4.0 International License