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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1993-3-11
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L03649,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L03650,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L03651,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L03652,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L03653,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L03654,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M98326,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M98327,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X59414,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/Z14124
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pubmed:abstractText |
A fragment of the cDNA encoding a rat valyl-tRNA synthetase (TrsVal)-like protein was cloned from a rat cDNA library in lambda gt11 using an oligodeoxyribonucleotide (oligo) probe. Three independent plaque clones containing the human TrsVal cDNA were then isolated from a lambda gt10 human erythroleukemia cDNA library using the rat cDNA fragment as the hybridization probe. Sequence analyses of the cDNA fragments provided a 3.2-kb sequence with an open reading frame that contained the 'HIGH' synthetase signature sequence and the tRNA 3'-end-binding motif, KMSKS, and putative Val-binding motif, EWCISRQ. The sequence was extended to the 3' end of the cDNA by the polymerase chain reaction using an internal primer and an oligo(dT) adapter. The deduced 1051-amino-acid sequence shares 65% identity with yeast TrsVal, and contains a highly basic N-terminal region, a newly evolved protease-sensitive region in sequence close to the C terminus, and several sites for protein kinase C phosphorylation. A 3-kb cDNA fragment was sub-cloned into plasmid pSVL and expressed in COS-7 cells; up to a sevenfold increase in TrsVal activity was obtained. These results confirm the cloning and sequencing of a human TrsVal-encoding cDNA.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0378-1119
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
123
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pubmed:geneSymbol |
Trs<up>Val</up>
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
181-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8428657-Amino Acid Sequence,
pubmed-meshheading:8428657-Animals,
pubmed-meshheading:8428657-Base Sequence,
pubmed-meshheading:8428657-Cloning, Molecular,
pubmed-meshheading:8428657-Gene Library,
pubmed-meshheading:8428657-Humans,
pubmed-meshheading:8428657-Molecular Sequence Data,
pubmed-meshheading:8428657-Rats,
pubmed-meshheading:8428657-Sequence Homology, Amino Acid,
pubmed-meshheading:8428657-Transfection,
pubmed-meshheading:8428657-Valine-tRNA Ligase
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pubmed:year |
1993
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pubmed:articleTitle |
Cloning, sequencing and expression of a cDNA encoding mammalian valyl-tRNA synthetase.
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pubmed:affiliation |
Department of Chemistry, Georgetown University, Washington, DC 20057.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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