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| pubmed-article:7511814 | lifeskim:mentions | umls-concept:C0035668 | lld:lifeskim |
| pubmed-article:7511814 | lifeskim:mentions | umls-concept:C0162807 | lld:lifeskim |
| pubmed-article:7511814 | lifeskim:mentions | umls-concept:C0073243 | lld:lifeskim |
| pubmed-article:7511814 | lifeskim:mentions | umls-concept:C0600499 | lld:lifeskim |
| pubmed-article:7511814 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:7511814 | pubmed:dateCreated | 1994-5-5 | lld:pubmed |
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| pubmed-article:7511814 | pubmed:abstractText | Phylogenetic comparative analyses of RNase P RNA-encoding gene sequences from Chlorobium limicola, Chlorobium tepidum, Bacteroides thetaiotaomicron, and Flavobacterium yabuuchiae refine the secondary structure model of the general (eu)bacterial RNase P RNA and show that a highly conserved feature of that RNA is not essential. Two helices, comprised of 2 base pairs each, are added to the secondary structure model and form part of a cruciform in the RNA. Novel sequence variations in the B. thetaiotaomicron and F. yabuuchiae RNA indicate the likelihood that all secondary structure resulting from canonical base-pairing has been detected: there are no remaining unpaired, contiguous, canonical complementarities in the structure model common to all bacterial RNase P RNAs. A nomenclature for the elements of the completed secondary structure model is proposed. The Chlorobium RNase P RNAs lack a stem-loop structure that is otherwise universally present and highly conserved in structure in other (eu)bacterial RNase P RNAs. The Chlorobium RNAs are nevertheless catalytic, with kinetic properties similar to those of RNase P RNAs of Escherichia coli and other Bacteria. Removal of this stem-loop structure from the E. coli RNA affects neither its affinity for nor its catalytic rate for cleavage of a precursor transfer RNA substrate. These results show that this structural element does not play a direct role in substrate binding or catalysis. | lld:pubmed |
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| pubmed-article:7511814 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7511814 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7511814 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7511814 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:7511814 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:7511814 | pubmed:author | pubmed-author:BrownJ WJW | lld:pubmed |
| pubmed-article:7511814 | pubmed:author | pubmed-author:PaceN RNR | lld:pubmed |
| pubmed-article:7511814 | pubmed:author | pubmed-author:PitulleCC | lld:pubmed |
| pubmed-article:7511814 | pubmed:author | pubmed-author:HaasE SES | lld:pubmed |
| pubmed-article:7511814 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7511814 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:7511814 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:7511814 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7511814 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7511814 | pubmed:pagination | 2527-31 | lld:pubmed |
| pubmed-article:7511814 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7511814 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7511814 | pubmed:articleTitle | Further perspective on the catalytic core and secondary structure of ribonuclease P RNA. | lld:pubmed |
| pubmed-article:7511814 | pubmed:affiliation | Department of Biology, Indiana University, Bloomington 47405. | lld:pubmed |
| pubmed-article:7511814 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7511814 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7511814 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7511814 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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