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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1994-5-5
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pubmed:databankReference |
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-1282240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-1370627,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-1371871,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-1374553,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-1375791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-1689306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-1700778,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-1701142,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-1711030,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-1719634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-2112744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-2421917,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-2423526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-2448875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-2449969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-2798413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-3122322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-3167979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-3658691,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-3881765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-6197186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-6246368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-7678561,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-7680125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-7690469,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7511814-8459849
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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:month |
Mar
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2527-31
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7511814-Bacteria,
pubmed-meshheading:7511814-Bacteroides,
pubmed-meshheading:7511814-Base Sequence,
pubmed-meshheading:7511814-Catalysis,
pubmed-meshheading:7511814-Cloning, Molecular,
pubmed-meshheading:7511814-Endoribonucleases,
pubmed-meshheading:7511814-Escherichia coli Proteins,
pubmed-meshheading:7511814-Flavobacterium,
pubmed-meshheading:7511814-Genes, Bacterial,
pubmed-meshheading:7511814-Molecular Sequence Data,
pubmed-meshheading:7511814-Nucleic Acid Conformation,
pubmed-meshheading:7511814-RNA, Bacterial,
pubmed-meshheading:7511814-RNA, Catalytic,
pubmed-meshheading:7511814-Ribonuclease P,
pubmed-meshheading:7511814-Sequence Homology, Nucleic Acid
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pubmed:year |
1994
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pubmed:articleTitle |
Further perspective on the catalytic core and secondary structure of ribonuclease P RNA.
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pubmed:affiliation |
Department of Biology, Indiana University, Bloomington 47405.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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