Substrate recognition by ribonucleoprotein ribonuclease MRP
| Autor: | Chao Quan, Andrey S. Krasilnikov, Anna Perederina, Igor Berezin, Olga Esakova |
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| Rok vydání: | 2010 |
| Předmět: |
Protein Conformation
RNase P Molecular Sequence Data Endoribonuclease Saccharomyces cerevisiae Biology RNase PH Article Substrate Specificity RNA Transfer stomatognathic system Endoribonucleases RNA Precursors Ribonuclease III RNase H Molecular Biology Ribonucleoprotein Binding Sites Base Sequence RNA Fungal Non-coding RNA Molecular biology RNase MRP Biochemistry biology.protein RNA |
| Zdroj: | RNA. 17:356-364 |
| ISSN: | 1469-9001 1355-8382 |
| Popis: | The ribonucleoprotein complex ribonuclease (RNase) MRP is a site-specific endoribonuclease essential for the survival of the eukaryotic cell. RNase MRP closely resembles RNase P (a universal endoribonuclease responsible for the maturation of the 5′ ends of tRNA) but recognizes distinct substrates including pre-rRNA and mRNA. Here we report the results of an in vitro selection of Saccharomyces cerevisiae RNase MRP substrates starting from a pool of random sequences. The results indicate that RNase MRP cleaves single-stranded RNA and is sensitive to sequences in the immediate vicinity of the cleavage site requiring a cytosine at the position +4 relative to the cleavage site. Structural implications of the differences in substrate recognition by RNases P and MRP are discussed. |
| Databáze: | OpenAIRE |
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