Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA
Abstract
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 Candida glabrata, the internal loop of helix P3 is 100% conserved between MRP and P RNAs. The helix P8 of MRP RNA from microsporidia Encephalitozoon cuniculi 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 Dictyostelium discoideum. 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.
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Footnotes
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↵1 These authors contributed to this paper equally.
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SUPPLEMENTAL MATERIALS Supplementary materials are available upon request from Yong Li, at yong.li{at}louisville.edu.
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Reprint requests to: Yong Li, Department of Biochemistry and Molecular Biology, and Center for Genetics and Molecular Medicine, School of Medicine, University of Louisville, 319 Abraham Flexner Way, Louisville, KY 40202, USA; e-mail: yong.li{at}louisville.edu; fax: (502) 852-6222.
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Article published online ahead of print. Article and publication date are at http://www.rnajournal.org/cgi/doi/10.1261/rna.2284906.
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- Received November 7, 2005.
- Accepted January 30, 2006.
- Copyright © 2006 RNA Society
