Linked Life Data

10594373

Source:http://linkedlifedata.com/resource/pubmed/id/10594373

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
2000-2-14
pubmed:abstractText
Early biochemical data showed that aminoacyl-tRNA synthetases often displayed species-specific recognition of tRNA. We compared the ability of purified Saccharomyces cerevisiae and Escherichia coli arginyl-tRNA synthetases to aminoacylate native and transcribed yeast tRNA(Arg) as well as E. coli tRNA(Arg). The kinetic data revealed that yeast ArgRS could charge E. coli tRNA(Arg), but at a lower efficiency than it charged either the transcribed or native yeast tRNA(Arg). E. coli ArgRS can acylate only its cognate E. coli tRNA. Strikingly, a single base change from C to A at position 20 in yeast tRNA(3)(Arg) altered the species specificity. The transcript of yeast tRNA(3)(Arg)CA20 mutant was aminoacylated by E. coli ArgRS with a 10(6) increase in k(cat)/K(m) over that for aminoacylation of yeast tRNA(3)(Arg) transcript. This indicates that A20 is not only an important identity of E. coli tRNA(Arg), but is also the key to altering species-specific aminoacylation of yeast tRNA(Arg).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
1473
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
356-62
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
A single base substitution in the variable pocket of yeast tRNA(Arg) eliminates species-specific aminoacylation.
pubmed:affiliation
State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry, Academia Sinica, 320 Yue-yang Road, Shanghai, China.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't