Linked Life Data

3144042

Source:http://linkedlifedata.com/resource/pubmed/id/3144042

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4885
pubmed:dateCreated
1989-1-25
pubmed:abstractText
The fidelity of protein biosynthesis in any cell rests on the accuracy of aminoacylation of tRNA. The exquisite specificity of this reaction is critically dependent on the correct recognition of tRNA by aminoacyl-tRNA synthetases. It is shown here that the relative concentrations of a tRNA and its cognate aminoacyl-tRNA synthetase are normally well balanced and crucial for maintenance of accurate aminoacylation. When Escherichia coli Gln-tRNA synthetase is overproduced in vivo, it incorrectly acylates the supF amber suppressor tRNA(Tyr) with Gln. This effect is abolished when the intracellular concentration of the cognate tRNA(Gln2) is also elevate. These data indicate that the presence of aminoacyl-tRNA synthetase and the cognate tRNAs in complexed form, which requires the proper balance of the two macromolecules, is critical in maintaining the fidelity of protein biosynthesis. Thus, limits exist on the relative levels of tRNAs and aminoacyl-tRNA synthetases within a cell.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
242
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1548-51
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Accuracy of in vivo aminoacylation requires proper balance of tRNA and aminoacyl-tRNA synthetase.
pubmed:affiliation
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.