In vitro study of E. coli tRNA identity elements
- PMID: 1283903
In vitro study of E. coli tRNA identity elements
Abstract
Various tRNA transcripts were constructed to study the identity elements of E. coli tRNAs (Arg, Lys, Ala, Trp, Thr, Gly, Ser, Asn, Cys, His). Anticodon are involved in the identity elements in these tRNA species except the case of tRNA(Ala) and tRNA(Ser). Especially, the second and third positions of the anticodon are the recognition sites of E. coli tRNA(Arg), tRNA(Lys) and tRNA(Thr) for their cognate aminoacyl-tRNA synthetases. Discriminator base is an identity determinant of the above examined tRNAs except tRNA(Thr) and tRNA(Ser). In some cases, acceptor stem (Thr, Gly, His) and variable pocket (Arg, Ala) are considered to be the recognition elements.
Similar articles
-
Identity determinants of E. coli tRNAs.Nucleic Acids Symp Ser. 1991;(25):153-4. Nucleic Acids Symp Ser. 1991. PMID: 1726805
-
Anticodon and acceptor stem nucleotides in tRNA(Gln) are major recognition elements for E. coli glutaminyl-tRNA synthetase.Nature. 1991 Jul 18;352(6332):258-60. doi: 10.1038/352258a0. Nature. 1991. PMID: 1857423
-
Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases.J Mol Biol. 2000 Jun 2;299(2):431-46. doi: 10.1006/jmbi.2000.3749. J Mol Biol. 2000. PMID: 10860750
-
[Role of the anticodon in recognition of tRNA by aminoacyl-tRNA-synthetases].Mol Biol (Mosk). 1983 Sep-Oct;17(5):928-48. Mol Biol (Mosk). 1983. PMID: 6355823 Review. Russian.
-
[The tRNA anticodon is recognized by aminoacyl-tRNA-synthetase].Mol Biol (Mosk). 1989 Nov-Dec;23(6):1603-10. Mol Biol (Mosk). 1989. PMID: 2698995 Review. Russian.
Cited by
-
The Enzymatic Paradox of Yeast Arginyl-tRNA Synthetase: Exclusive Arginine Transfer Controlled by a Flexible Mechanism of tRNA Recognition.PLoS One. 2016 Feb 4;11(2):e0148460. doi: 10.1371/journal.pone.0148460. eCollection 2016. PLoS One. 2016. PMID: 26844776 Free PMC article.