rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
1990-6-4
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pubmed:abstractText |
Two Bacillus subtilis tRNA(His) precursors (Green, C. J., and Vold, B. S. (1988) J. Biol. Chem. 263, 652-657) were processed by Escherichia coli RNase P in the presence of varying [Mg2+]. The wild type precursor was processed under all conditions to afford a single tRNA product containing 8 base pairs in the acceptor stem. In contrast, the position of processing of a mutant tRNA(His) precursor (containing a G27----A27 alteration) was shown to be condition-dependent. Processing occurred at A27 under conditions consistent with formation of an A27-C100 base pair in the acceptor stem but at G28 under conditions that disfavored base pair formation. The ability to control the site of RNase P-mediated tRNA precursor processing is unprecedented and permits analysis of the chemical factors that promote processing.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acid-Specific,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, His,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease P,
http://linkedlifedata.com/resource/pubmed/chemical/ribonuclease P, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
265
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7100-3
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2110159-Bacillus subtilis,
pubmed-meshheading:2110159-Base Sequence,
pubmed-meshheading:2110159-Endoribonucleases,
pubmed-meshheading:2110159-Escherichia coli Proteins,
pubmed-meshheading:2110159-Kinetics,
pubmed-meshheading:2110159-Magnesium,
pubmed-meshheading:2110159-Molecular Sequence Data,
pubmed-meshheading:2110159-Mutation,
pubmed-meshheading:2110159-Nucleic Acid Conformation,
pubmed-meshheading:2110159-RNA, Transfer, Amino Acid-Specific,
pubmed-meshheading:2110159-RNA, Transfer, His,
pubmed-meshheading:2110159-RNA Processing, Post-Transcriptional,
pubmed-meshheading:2110159-Ribonuclease P,
pubmed-meshheading:2110159-Substrate Specificity,
pubmed-meshheading:2110159-Thermodynamics,
pubmed-meshheading:2110159-Transcription, Genetic
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pubmed:year |
1990
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pubmed:articleTitle |
Control of the position of RNase P-mediated transfer RNA precursor processing.
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pubmed:affiliation |
Department of Chemistry, University of Virginia, Charlottesville 22901.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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