Publication Date:
1988-12-16
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Swanson, R -- Hoben, P -- Sumner-Smith, M -- Uemura, H -- Watson, L -- Soll, D -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1548-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3144042" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acyl-tRNA Synthetases/genetics/*metabolism
;
Escherichia coli/enzymology/*genetics
;
Kinetics
;
Plasmids
;
RNA, Transfer, Amino Acid-Specific/*metabolism
;
RNA, Transfer, Gln/*metabolism
;
beta-Galactosidase/genetics/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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