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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2-3
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pubmed:dateCreated |
1997-2-6
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pubmed:abstractText |
RNase P recognizes many different precursor tRNAs as well as other substrates and cleaves all of them accurately at the expected position. RNase P recognizes the tRNA structure of the precursor tRNA by a set of interactions between the catalytic RNA subunit and the T- and acceptor-stems mainly, although residues in the 5'-leader sequence as well as the 3'-terminal CCA are important. These conclusions have been reached by several studies on mutant precursor tRNAs as well as cross-linking studies between RNase P RNA and precursor tRNAs. The protein subunit of RNase P seems also to affect the way that the substrate is recognized as well as the range of substrates that can be used by RNase P, although the protein does not seem to interact directly with the substrates. The interaction between the protein and RNA subunits of RNase P has been extensively studied in vitro. The protein subunit sequence is not highly conserved among bacteria, however different proteins are functionally equivalent as heterologous reconstitution of the RNase P holoenzyme can be achieved in many cases.
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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/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Catalytic,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease P,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/ribonuclease P, E coli
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pubmed:status |
MEDLINE
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pubmed:issn |
0301-4851
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
99-109
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8901495-Amino Acid Sequence,
pubmed-meshheading:8901495-Bacteria,
pubmed-meshheading:8901495-Base Sequence,
pubmed-meshheading:8901495-Conserved Sequence,
pubmed-meshheading:8901495-Endoribonucleases,
pubmed-meshheading:8901495-Escherichia coli,
pubmed-meshheading:8901495-Escherichia coli Proteins,
pubmed-meshheading:8901495-Macromolecular Substances,
pubmed-meshheading:8901495-Molecular Sequence Data,
pubmed-meshheading:8901495-Mutagenesis,
pubmed-meshheading:8901495-Nucleic Acid Conformation,
pubmed-meshheading:8901495-RNA, Bacterial,
pubmed-meshheading:8901495-RNA, Catalytic,
pubmed-meshheading:8901495-RNA, Transfer,
pubmed-meshheading:8901495-RNA Precursors,
pubmed-meshheading:8901495-RNA Processing, Post-Transcriptional,
pubmed-meshheading:8901495-Ribonuclease P,
pubmed-meshheading:8901495-Ribonucleoproteins,
pubmed-meshheading:8901495-Sequence Homology, Amino Acid,
pubmed-meshheading:8901495-Substrate Specificity
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pubmed:articleTitle |
RNase P from bacteria. Substrate recognition and function of the protein subunit.
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pubmed:affiliation |
Department of Microbiology, Biomedical Center, Uppsala, Sweden.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Review,
Research Support, Non-U.S. Gov't
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