The P3 domain ofE. coliribonuclease P RNA can be truncated and replaced
| Autor: | Yo Kikuchi, Naomi Kanda, Terumichi Tanaka |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
RNase P
Molecular Sequence Data Biophysics medicine.disease_cause Biochemistry RNase PH Ribonuclease P Ribozyme Structural Biology P3 domain Escherichia coli Genetics medicine Ribonuclease III RNase H Molecular Biology Phylogeny Base Sequence biology Chemistry E. coli RNA Cell Biology Molecular biology RNA Bacterial Holoenzyme RNase MRP biology.protein Nucleic Acid Conformation |
| Zdroj: | FEBS Letters. 577:101-104 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2004.09.072 |
| Popis: | We prepared some truncated and replaced P3 mutants of Escherichia coli RNase P RNA, and used them to examine the RNase P ribozyme and holoenzyme reactions of a pre-tRNA substrate. The results indicated that mutations in the P3 domain did not affect the cleavage site selection of the pre-tRNA substrate, but did affect the efficiency of cleavage of the substrate. Results of stepwise truncation of the P3 domain and its replacement by the TAR sequence showed that the P3 domain of the E. coli RNase P was able to be truncated to certain length and was replaceable, but could not be deleted in the ribozyme. |
| Databáze: | OpenAIRE |
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