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rdf:type |
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lifeskim:mentions |
umls-concept:C0014442,
umls-concept:C0021941,
umls-concept:C0043393,
umls-concept:C0073243,
umls-concept:C0086418,
umls-concept:C0290741,
umls-concept:C0332120,
umls-concept:C0599220,
umls-concept:C0919458,
umls-concept:C0936012,
umls-concept:C1334043,
umls-concept:C1537665,
umls-concept:C1704873,
umls-concept:C1825410,
umls-concept:C1999230,
umls-concept:C2697616
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pubmed:issue |
18
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pubmed:dateCreated |
2006-11-3
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pubmed:abstractText |
The RNases P and MRP are involved in tRNA and rRNA processing, respectively. Both enzymes in eukaryotes are composed of an RNA molecule and 9-12 protein subunits. Most of the protein subunits are shared between RNases P and MRP. We have here performed a computational analysis of the protein subunits in a broad range of eukaryotic organisms using profile-based searches and phylogenetic methods. A number of novel homologues were identified, giving rise to a more complete inventory of RNase P/MRP proteins. We present evidence of a relationship between fungal Pop8 and the protein subunit families Rpp14/Pop5 as well as between fungal Pop6 and metazoan Rpp25. These relationships further emphasize a structural and functional similarity between the yeast and human P/MRP complexes. We have also identified novel P and MRP RNAs and analysis of all available sequences revealed a K-turn motif in a large number of these RNAs. We suggest that this motif is a binding site for the Pop3/Rpp38 proteins and we discuss other structural features of the RNA subunit and possible relationships to the protein subunit repertoire.
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pubmed:commentsCorrections |
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16998185-9918945
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1362-4962
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
34
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5145-56
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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