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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1988-4-14
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pubmed:databankReference |
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pubmed:abstractText |
Secondary structure models for the ribonuclease (RNAase) P RNAs of Bacillus subtilis and E. coli were derived by a phylogenetic comparative analysis of published sequences as well as four novel ones. The RNAase P RNA genes from Bacillus megaterium, Bacillus brevis, Bacillus stearothermophilus, and Pseudomonas fluorescens were cloned, sequenced, and compared with the other available sequences. Regions of pairing were identified by the occurrence of homologous complementary sequences that vary among the compared molecules. A common core of primary and secondary structure can be identified in all these RNAase P RNAs. The previously noted striking differences between the Bacillus and the enteric RNAase P RNAs arise not only from point mutations, but from the addition or deletion of structural domains. The primary and secondary structural features that are common to all of the RNAase P RNAs are likely to be the elements involved in the binding and cleavage of tRNA precursors, and in the interaction with the RNAase P protein.
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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/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Catalytic,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal,
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 |
Jan
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
52
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
19-26
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2449969-Bacillus,
pubmed-meshheading:2449969-Bacillus subtilis,
pubmed-meshheading:2449969-Base Sequence,
pubmed-meshheading:2449969-Cloning, Molecular,
pubmed-meshheading:2449969-DNA, Bacterial,
pubmed-meshheading:2449969-Endoribonucleases,
pubmed-meshheading:2449969-Escherichia coli,
pubmed-meshheading:2449969-Escherichia coli Proteins,
pubmed-meshheading:2449969-Genes, Bacterial,
pubmed-meshheading:2449969-Genetic Variation,
pubmed-meshheading:2449969-Molecular Sequence Data,
pubmed-meshheading:2449969-Nucleic Acid Conformation,
pubmed-meshheading:2449969-Nucleic Acid Hybridization,
pubmed-meshheading:2449969-Pseudomonas fluorescens,
pubmed-meshheading:2449969-RNA, Bacterial,
pubmed-meshheading:2449969-RNA, Catalytic,
pubmed-meshheading:2449969-RNA, Ribosomal,
pubmed-meshheading:2449969-Ribonuclease P,
pubmed-meshheading:2449969-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2449969-Transcription, Genetic
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pubmed:year |
1988
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pubmed:articleTitle |
The secondary structure of ribonuclease P RNA, the catalytic element of a ribonucleoprotein enzyme.
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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.
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