rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1994-9-8
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pubmed:databankReference |
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pubmed:abstractText |
Characterization of the RNase P RNA gene derived from Borrelia burgdorferi reveals covariation of the conserved nucleotides at positions corresponding to nucleotides 128 and 230 in Escherichia coli RNase P RNA (M1 RNA). Single base substitutions at either of these positions in M1 RNA resulted in a lack of complementation of the temperature-sensitive phenotype associated with rnpA49 in vivo whereas complementation was observed for the double mutant M1 RNA or wild-type M1 RNA. Our in vitro data showed that M1 RNA harbouring a substitution at 128 or 230 cleaved a tRNA precursor both in the absence and presence of C5 with reduced efficiency compared to the wild-type and the double mutant M1 RNA. We conclude that the nucleotides at positions 128 and 230 establish a long-range tertiary interaction in RNase P RNA. Our data also suggest that this interaction together with the identity of the nucleotide at position 230 is important for Pb2+ induced cleavage at specific positions in M1 RNA.
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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/Lead,
http://linkedlifedata.com/resource/pubmed/chemical/Organometallic Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Catalytic,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Tyr,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease P,
http://linkedlifedata.com/resource/pubmed/chemical/lead acetate,
http://linkedlifedata.com/resource/pubmed/chemical/ribonuclease P, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0022-2836
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
241
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7519680-Base Sequence,
pubmed-meshheading:7519680-Borrelia burgdorferi Group,
pubmed-meshheading:7519680-Cloning, Molecular,
pubmed-meshheading:7519680-Endoribonucleases,
pubmed-meshheading:7519680-Escherichia coli Proteins,
pubmed-meshheading:7519680-Genes, Bacterial,
pubmed-meshheading:7519680-Lead,
pubmed-meshheading:7519680-Molecular Sequence Data,
pubmed-meshheading:7519680-Nucleic Acid Conformation,
pubmed-meshheading:7519680-Organometallic Compounds,
pubmed-meshheading:7519680-Point Mutation,
pubmed-meshheading:7519680-RNA, Bacterial,
pubmed-meshheading:7519680-RNA, Catalytic,
pubmed-meshheading:7519680-RNA, Transfer, Tyr,
pubmed-meshheading:7519680-Ribonuclease P
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pubmed:year |
1994
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pubmed:articleTitle |
Characterization of the Borrelia burgdorferi RNase P RNA gene reveals a novel tertiary interaction.
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pubmed:affiliation |
National Veterinary Institute, Uppsala, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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