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Secondary structure of RNase MRP RNA as predicted by phylogenetic comparison
Author(s) -
Schmitt Mark E.,
Bennett Jeffery L.,
Dairaghi Daniel J.,
Clayton David A.
Publication year - 1993
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.7.1.7678563
Subject(s) - rnase mrp , rnase p , endoribonuclease , rna , rnase ph , rnase h , biology , ribonuclease iii , non coding rna , ribonucleoprotein , microbiology and biotechnology , genetics , gene , rna interference
RNase MRP is a ribonucleoprotein endoribonuclease that has been shown to cleave mitochondrial primer RNA sequences from a variety of sources. The bulk of RNase MRP activity is found in the nucleus where its function remains unknown. Two different approaches have resulted in predictions of distinct secondary structures for RNase MRP RNA. In order to analyze more definitively the higher‐order structure of RNase MRP RNA, we have conducted a phylogenetic comparison of the available RNase MRP RNA sequences from human, mouse, rat, cow, toad, and yeast. The resulting secondary structure shares features in common with previously described structures for prokaryotic and eukaryotic RNase P RNAs (1) and RNase MRP RNAs (2, 3). In addition, the phylogenetic structure is consistent with available chemical modification data on RNase MRP RNA and with the detailed analysis of the To antigen binding domain located near the 5′ end of the RNase MRP RNA. The structure is not limited to RNase MRP RNAs, but can be expanded to cover both eukaryotic RNase P RNAs and RNase P/MRP RNAs from plants.— Schmitt, M. E., Bennett, J. L., Dairaghi, D. J., Clayton, D. A. Secondary structure of RNase MRP RNA as predicted by phylogenetic comparison. FASEB J. 7: 208‐213; 1993.