Abstract
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.
Publication types
-
Comparative Study
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Base Sequence
-
DNA-Directed RNA Polymerases / metabolism
-
Endoribonucleases / metabolism*
-
Kinetics
-
Models, Structural
-
Molecular Sequence Data
-
Mutagenesis
-
Nucleic Acid Conformation*
-
RNA Precursors / chemistry*
-
RNA Precursors / metabolism*
-
RNA, Catalytic / metabolism*
-
RNA, Transfer, Phe / chemistry*
-
RNA, Transfer, Phe / metabolism*
-
Ribonuclease P
-
Substrate Specificity
-
Templates, Genetic
-
Transcription, Genetic
-
Viral Proteins
-
Xenopus laevis
Substances
-
RNA Precursors
-
RNA, Catalytic
-
RNA, Transfer, Phe
-
Viral Proteins
-
bacteriophage T7 RNA polymerase
-
DNA-Directed RNA Polymerases
-
Endoribonucleases
-
Ribonuclease P