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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
|
pubmed:dateCreated |
1985-1-14
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pubmed:abstractText |
Although aminoacyl-tRNA synthetases catalyze the same chemical reaction, the individual enzymes have a wide range of sizes. Proteolytic digestion has yielded active catalytic fragments of two synthetases. A set of gene deletions in a large synthetase has been used successfully in the creation of a variety of enzyme fragments that have been studied individually; a fragment with about half of the total polypeptide is sufficient to aminoacylate tRNA in vivo. The results suggest that size polymorphism is caused by fusion, to a core catalytic segment, of variable amounts of additional polypeptide sequences. These sequences may serve to impart additional functions. For example, in one case, a synthetase binds to its own gene promoter and regulates transcription.
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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 |
Dec
|
pubmed:issn |
0014-9446
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
43
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2987-90
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading | |
pubmed:year |
1984
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pubmed:articleTitle |
Size polymorphism and the structure of aminoacyl-tRNA synthetases.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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