doi: 10.1073/pnas.74.6.2246.
Experimental evidence for kinetic proofreading in the aminoacylation of tRNA by synthetase
- PMID: 329276
- PMCID: PMC432146
- DOI: 10.1073/pnas.74.6.2246
Item in Clipboard
Experimental evidence for kinetic proofreading in the aminoacylation of tRNA by synthetase
Proc Natl Acad Sci U S A.
1977 Jun.
Abstract
The enzymatic aminoacylation of tRNA can be viewed as a means of proofreading either the amino acid or the tRNA or both. We have conducted further experimental tests of kinetic proofreading in discriminating between cognate and noncognate amino acids and tRNAs as follows: (formula: see text). In cases (i) and (ii) the amino acids are proofread, in cases (iii) and (iv) the tRNA is proofread, and in case (v), both the amino acid and the tRNA are proofread. ATP consumed per acylation was 400, 1.5, 40, 25, and 1000, respectively. High ATP/aminoacylation ratios are diagnostic for kinetic proofreading.
Similar articles
-
Hydrolytic action of aminoacyl-tRNA synthetases from baker's yeast: "chemical proofreading" preventing acylation of tRNA(I1e) with misactivated valine.Biochemistry. 1976 Sep 7;15(18):4131-8. doi: 10.1021/bi00663a034. Biochemistry. 1976. PMID: 786367
-
Aminoacyl-tRNA synthetases from baker's yeast: reacting site of enzymatic aminoacylation is not uniform for all tRNAs.FEBS Lett. 1975 Aug 15;56(2):212-4. doi: 10.1016/0014-5793(75)81093-3. FEBS Lett. 1975. PMID: 1098930 No abstract available.
-
Valyl-tRNA, isoleucyl-tRNA and tyrosyl-tRNA synthetase from baker's yeast. Substrate specificity with regard to ATP analogs and mechanism of the aminoacylation reaction.Eur J Biochem. 1976 Jul 15;66(3):493-7. doi: 10.1111/j.1432-1033.1976.tb10574.x. Eur J Biochem. 1976. PMID: 782885
-
[Superspecificity of aminoacyl-tRNA-synthases].Mol Biol (Mosk). 1984 Jan-Feb;18(1):205-26. Mol Biol (Mosk). 1984. PMID: 6423966 Review. Russian.
-
Synthetic and editing reactions of aminoacyl-tRNA synthetases using cognate and non-cognate amino acid substrates.Methods. 2017 Jan 15;113:13-26. doi: 10.1016/j.ymeth.2016.09.015. Epub 2016 Oct 3. Methods. 2017. PMID: 27713080 Review.
Cited by
-
Preferential hydrophobic interactions are responsible for a preference of D-amino acids in the aminoacylation of 5'-AMP with hydrophobic amino acids.Experientia. 1992 Apr 15;48(4):379-83. doi: 10.1007/BF01923434. Experientia. 1992. PMID: 1582495
-
Proofreading in vivo: editing of homocysteine by methionyl-tRNA synthetase in Escherichia coli.Proc Natl Acad Sci U S A. 1990 Jun;87(12):4504-8. doi: 10.1073/pnas.87.12.4504. Proc Natl Acad Sci U S A. 1990. PMID: 2191291 Free PMC article.
-
Differential distribution of D and L amino acids between the 2' and 3' positions of the AMP residue at the 3' terminus of transfer ribonucleic acid.Proc Natl Acad Sci U S A. 1988 Jul;85(14):4996-5000. doi: 10.1073/pnas.85.14.4996. Proc Natl Acad Sci U S A. 1988. PMID: 3393527 Free PMC article.
-
Implications of treadmilling for the stability and polarity of actin and tubulin polymers in vivo.J Cell Biol. 1980 Jul;86(1):330-4. doi: 10.1083/jcb.86.1.330. J Cell Biol. 1980. PMID: 6893454 Free PMC article.
-
Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus. 2016 May;7(1):10.1128/ecosalplus.ESP-0002-2016. doi: 10.1128/ecosalplus.ESP-0002-2016. EcoSal Plus. 2016. PMID: 27223819 Free PMC article. Review.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
