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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
1994-7-7
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pubmed:abstractText |
Imino 15N and 1H resonances of Escherichia coli tRNA(lIle) were observed in the absence and presence of E coli isoleucyl-tRNA synthetase. Upon complex formation of tRNA(lIle) with isoleucyl-tRNA synthetase, some imino 15N-1H resonances disappeared, and some others were significantly broadened and/or shifted in the 1H chemical shift, while the others were observed at the same 15N-1H chemical shifts. It was indicated that the binding of tRNA(lIle) with IleRS affect the following four regions: the anticodon stem, the junction of the acceptor and T stems, the middle of the D stem, and the region where the tertiary base pair connects the T, D, and extra loops. This result is consistent with those of chemical footprinting and site-directed mutagenesis studies. Taken together, these three independent results reveal the recognition mechanism of tRNA(lIle) by IleRS: IleRS recognizes all the identity determinants distributed throughout the tRNA(lIle) molecule, which induces changes in the secondary and tertiary structures of tRNA(lIle).
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:issn |
0300-9084
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
75
|
pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1109-15
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8199246-Base Sequence,
pubmed-meshheading:8199246-Binding Sites,
pubmed-meshheading:8199246-Escherichia coli,
pubmed-meshheading:8199246-Isoleucine-tRNA Ligase,
pubmed-meshheading:8199246-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8199246-Molecular Sequence Data,
pubmed-meshheading:8199246-Nucleic Acid Conformation,
pubmed-meshheading:8199246-RNA, Transfer, Ile
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pubmed:year |
1993
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pubmed:articleTitle |
A 15N-1H nuclear magnetic resonance study on the interaction between isoleucine tRNA and isoleucyl-tRNA synthetase from Escherichia coli.
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pubmed:affiliation |
Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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