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Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA
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| Zeitschriftentitel: | RNA |
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| Personen und Körperschaften: | , , , |
| In: | RNA, 12, 2006, 5, S. 699-706 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Cold Spring Harbor Laboratory
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| Schlagwörter: |
| Zusammenfassung: | <jats:p>RNase MRP is a eukaryote-specific endoribonuclease that generates RNA primers for mitochondrial DNA replication and processes precursor rRNA. RNase P is a ubiquitous endoribonuclease that cleaves precursor tRNA transcripts to produce their mature 5′ termini. We found extensive sequence homology of catalytic domains and specificity domains between their RNA subunits in many organisms. In <jats:italic>Candida glabrata</jats:italic>, the internal loop of helix P3 is 100% conserved between MRP and P RNAs. The helix P8 of MRP RNA from microsporidia <jats:italic>Encephalitozoon cuniculi</jats:italic> is identical to that of P RNA. Sequence homology can be widely spread over the whole molecule of MRP RNA and P RNA, such as those from <jats:italic>Dictyostelium discoideum</jats:italic>. These conserved nucleotides between the MRP and P RNAs strongly support the hypothesis that the MRP RNA is derived from the P RNA molecule in early eukaryote evolution.</jats:p> |
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| Umfang: | 699-706 |
| ISSN: |
1355-8382
1469-9001 |
| DOI: | 10.1261/rna.2284906 |