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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1989-9-18
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pubmed:abstractText |
The reaction of wild-type and two mutant derivatives of RNase P have been examined with wild-type and mutant substrates. We show that a mutant derivative of tRNA(Tyr)Su3, tRNA(Tyr)Su3A15, in which the G15.C48(57) base-pair essential for folding of the tRNA moiety is altered, is a temperature-sensitive suppressor in vivo. The precursor to tRNA(Tyr)Su3A15 is cleaved in a temperature-sensitive manner in vitro by RNase P and with a higher Km compared to the precursor to tRNA(Tyr)Su3. The precursor to tRNA(Tyr)Su3A2, another temperature-sensitive suppressor in vivo in which the G2.C71(80) base-pair in the acceptor stem is changed to A2.C71(80), behaves like the precursor to tRNA(Tyr)Su3 in vitro; that is, it is not cleaved in a temperature-sensitive manner. Therefore, there are at least two ways in which a suppressor tRNA can acquire a temperature-sensitive phenotype in vivo. One of the mutant derivatives of RNase P we have tested, rnpA49, which affects the protein cofactor of the enzyme, has a decreased kcat compared to wild-type, which can explain its phenotype in vivo.
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pubmed:language |
eng
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pubmed:journal | |
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/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Tyr,
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 |
Jun
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
207
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
837-40
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2474662-Endoribonucleases,
pubmed-meshheading:2474662-Escherichia coli,
pubmed-meshheading:2474662-Escherichia coli Proteins,
pubmed-meshheading:2474662-Kinetics,
pubmed-meshheading:2474662-Mutation,
pubmed-meshheading:2474662-RNA, Bacterial,
pubmed-meshheading:2474662-RNA, Transfer, Tyr,
pubmed-meshheading:2474662-Ribonuclease P,
pubmed-meshheading:2474662-Temperature
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pubmed:year |
1989
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pubmed:articleTitle |
Reaction in vitro of some mutants of RNase P with wild-type and temperature-sensitive substrates.
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pubmed:affiliation |
Department of Biology, Yale University, New Haven, CT 06520.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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