Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1985-1-14
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-9446
pubmed:author
pubmed:issnType
Print
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2987-90
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Size polymorphism and the structure of aminoacyl-tRNA synthetases.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.