Open AccessTwo helices plus a linker: a small model substrate for eukaryotic RNase P.
Author(s) -
G. Carrara,
Patrizia Calandra,
Paolo Fruscoloni,
Glauco P. TocchiniValentini
Publication year - 1995
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.92.7.2627
Subject(s) - rnase p , linker , transfer rna , stem loop , rna , rnase ph , stem cell , biology , acceptor , chemistry , biochemistry , stereochemistry , microbiology and biotechnology , gene , physics , computer science , operating system , condensed matter physics
Using precursor tRNA molecules to study RNA-protein interactions, we have identified an RNA motif recognized by eukaryotic RNase P (EC 3.1.26.5). Analysis of circularly permuted precursors indicates that interruptions in the sugar-phosphate backbone are not tolerated in the acceptor stem, in the T stem-loop, or between residues A-9 and G-10. Prokaryotic RNase P will function with a minihelix consisting of the acceptor stem connected directly to the T stem-loop. Eukaryotic RNase P cannot use such a minimal substrate unless a linker sequence is added in the gap where the D stem and anticodon stem-loop were deleted.