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Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA
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| Zeitschriftentitel: | RNA |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | RNA, 12, 2006, 5, S. 699-706 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Cold Spring Harbor Laboratory
|
| Schlagwörter: |
| author_facet |
Zhu, Yanglong Stribinskis, Vilius Ramos, Kenneth S. Li, Yong Zhu, Yanglong Stribinskis, Vilius Ramos, Kenneth S. Li, Yong |
|---|---|
| author |
Zhu, Yanglong Stribinskis, Vilius Ramos, Kenneth S. Li, Yong |
| spellingShingle |
Zhu, Yanglong Stribinskis, Vilius Ramos, Kenneth S. Li, Yong RNA Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA Molecular Biology |
| author_sort |
zhu, yanglong |
| spelling |
Zhu, Yanglong Stribinskis, Vilius Ramos, Kenneth S. Li, Yong 1355-8382 1469-9001 Cold Spring Harbor Laboratory Molecular Biology http://dx.doi.org/10.1261/rna.2284906 <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> Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA RNA |
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10.1261/rna.2284906 |
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Cold Spring Harbor Laboratory, 2006 |
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Cold Spring Harbor Laboratory, 2006 |
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1355-8382 1469-9001 |
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RNA |
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| title |
Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA |
| title_unstemmed |
Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA |
| title_full |
Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA |
| title_fullStr |
Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA |
| title_full_unstemmed |
Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA |
| title_short |
Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA |
| title_sort |
sequence analysis of rnase mrp rna reveals its origination from eukaryotic rnase p rna |
| topic |
Molecular Biology |
| url |
http://dx.doi.org/10.1261/rna.2284906 |
| publishDate |
2006 |
| physical |
699-706 |
| description |
<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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| author | Zhu, Yanglong, Stribinskis, Vilius, Ramos, Kenneth S., Li, Yong |
| author_facet | Zhu, Yanglong, Stribinskis, Vilius, Ramos, Kenneth S., Li, Yong, Zhu, Yanglong, Stribinskis, Vilius, Ramos, Kenneth S., Li, Yong |
| author_sort | zhu, yanglong |
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| description | <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> |
| doi_str_mv | 10.1261/rna.2284906 |
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| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTI2MS9ybmEuMjI4NDkwNg |
| imprint | Cold Spring Harbor Laboratory, 2006 |
| imprint_str_mv | Cold Spring Harbor Laboratory, 2006 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
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| issn_str_mv | 1355-8382, 1469-9001 |
| language | English |
| last_indexed | 2024-03-01T16:17:46.667Z |
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| physical | 699-706 |
| publishDate | 2006 |
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| series | RNA |
| source_id | 49 |
| spelling | Zhu, Yanglong Stribinskis, Vilius Ramos, Kenneth S. Li, Yong 1355-8382 1469-9001 Cold Spring Harbor Laboratory Molecular Biology http://dx.doi.org/10.1261/rna.2284906 <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> Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA RNA |
| spellingShingle | Zhu, Yanglong, Stribinskis, Vilius, Ramos, Kenneth S., Li, Yong, RNA, Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA, Molecular Biology |
| title | Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA |
| title_full | Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA |
| title_fullStr | Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA |
| title_full_unstemmed | Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA |
| title_short | Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA |
| title_sort | sequence analysis of rnase mrp rna reveals its origination from eukaryotic rnase p rna |
| title_unstemmed | Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA |
| topic | Molecular Biology |
| url | http://dx.doi.org/10.1261/rna.2284906 |