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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
29
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pubmed:dateCreated |
1993-12-28
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pubmed:abstractText |
A variety of genetic, biochemical and structural studies have been used to determine factors ensuring the accuracy of recognition by aminoacyl-tRNA synthetases for tRNA. The identity elements of Escherichia coli tRNA(Gln) are located mainly in the anticodon and acceptor stem, and ensure the accurate recognition of the tRNA by glutaminyl-tRNA synthetase. We summarize a number of experimental techniques to define the accuracy of aminoacylation in vivo and in vitro.
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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 |
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pubmed:status |
MEDLINE
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pubmed:issn |
0261-3166
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
211-3
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:7504247-Amino Acyl-tRNA Synthetases,
pubmed-meshheading:7504247-Anticodon,
pubmed-meshheading:7504247-Base Sequence,
pubmed-meshheading:7504247-DNA Mutational Analysis,
pubmed-meshheading:7504247-Escherichia coli,
pubmed-meshheading:7504247-Molecular Sequence Data,
pubmed-meshheading:7504247-Nucleic Acid Conformation,
pubmed-meshheading:7504247-RNA, Bacterial,
pubmed-meshheading:7504247-RNA, Transfer, Glu
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pubmed:year |
1993
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pubmed:articleTitle |
The recognition of E. coli glutamine tRNA by glutaminyl-tRNA synthetase.
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pubmed:affiliation |
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
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pubmed:publicationType |
Journal Article
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