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rdf:type |
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lifeskim:mentions |
|
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pubmed:issue |
2
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pubmed:dateCreated |
1992-5-15
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pubmed:abstractText |
Interferon gamma induces expression of a protein termed IFP 53 according to its molecular weight of 53 kDa. IFP 53 shows significant sequence homology to rabbit peptide chain release factor as well as to bovine tryptophanyl-tRNA synthetase. IFP 53 has been shown to possess release factor activity for the UGA stop codon. We demonstrate here, by using a recombinant IFP 53 fusion protein, that IFP 53 tryptophanylates tRNA. These data indicate that IFP 53 is a protein with two activities: peptide chain termination and aminoacylation.
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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:month |
Mar
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pubmed:issn |
0014-5793
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
30
|
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pubmed:volume |
300
|
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
162-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1373391-Acylation,
pubmed-meshheading:1373391-Amino Acid Sequence,
pubmed-meshheading:1373391-Blotting, Western,
pubmed-meshheading:1373391-Cloning, Molecular,
pubmed-meshheading:1373391-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1373391-Enzyme Induction,
pubmed-meshheading:1373391-HeLa Cells,
pubmed-meshheading:1373391-Humans,
pubmed-meshheading:1373391-Interferons,
pubmed-meshheading:1373391-Molecular Sequence Data,
pubmed-meshheading:1373391-Recombinant Fusion Proteins,
pubmed-meshheading:1373391-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1373391-Tryptophan-tRNA Ligase
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pubmed:year |
1992
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pubmed:articleTitle |
An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase.
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pubmed:affiliation |
Medical School Hannover, Institute for Medical Microbiology, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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