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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1993-2-5
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pubmed:abstractText |
The resistance of certain tumor cells to the chemotherapeutic agent L-asparaginase has often been found to be associated with the presence of asparagine synthetase activity. In an attempt to study the translational regulation of the asparagine synthetase gene, the 5'-untranslated region of human asparagine synthetase cDNA was mapped by antisense oligonucleotide-mediated hybrid arrest translation in reticulocyte lysate. Three consecutive cis-acting regulatory elements, spanning from -60 to -120 bases from the initiation codon, in the 5'-untranslated region of the asparagine synthetase gene, were identified. T1 RNase footprinting analysis showed that those regulatory elements can be protected from T1 digestion when incubated with reticulocyte lysate. A 46-kDa trans-acting protein factor that interacts with the cis-acting regulatory element of asparagine synthetase mRNA was detected. This 46-kDa protein factor is most likely to be the eucaryotic peptide chain initiation factor eIF-4A as determined by immunoprecipitation experiments using a monoclonal antibody raised against reticulocyte eIF-4A.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aspartate-Ammonia Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-4A,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Initiation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease T1
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1298-303
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8093451-Aspartate-Ammonia Ligase,
pubmed-meshheading:8093451-Base Sequence,
pubmed-meshheading:8093451-Binding Sites,
pubmed-meshheading:8093451-Eukaryotic Initiation Factor-4A,
pubmed-meshheading:8093451-Humans,
pubmed-meshheading:8093451-Molecular Sequence Data,
pubmed-meshheading:8093451-Oligodeoxyribonucleotides,
pubmed-meshheading:8093451-Peptide Initiation Factors,
pubmed-meshheading:8093451-Plasmids,
pubmed-meshheading:8093451-Protein Biosynthesis,
pubmed-meshheading:8093451-RNA, Messenger,
pubmed-meshheading:8093451-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:8093451-Restriction Mapping,
pubmed-meshheading:8093451-Ribonuclease T1,
pubmed-meshheading:8093451-Transcription, Genetic
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pubmed:year |
1993
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pubmed:articleTitle |
Interaction of the eucaryotic peptide chain initiation factor eIF-4A with the specific elements at the 5'-untranslated sequence of human asparagine synthetase mRNA.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Florida, Gainesville 32610.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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