Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Discrimination against misacylated tRNA by chloroplast elongation factor Tu.

Literature DB >> 8307009

Discrimination against misacylated tRNA by chloroplast elongation factor Tu.

Abstract

Chloroplast elongation factor Tu was purified from Pisum sativum and the binding properties of glutamylated chloroplast tRNAs were studied by gel-permeation chromatography. Whereas chloroplast Glu-tRNA(Glu) is efficiently bound by this factor, the misacylated Glu-tRNA(Gln) does not interact with chloroplast elongation factor Tu.GTP and is thus efficiently excluded from protein synthesis. Comparison with the behaviour of Escherichia coli elongation factor Tu.GTP shows that this factor, which is not confronted with the in vivo misacylation phenomenon of organelles, binds both Glu-tRNA(Glu) and Glu-tRNA(Gln) from chloroplasts with approximately equal efficiency.

Entities: Chemical Species

Mesh：

Substances：

Year: 1994 PMID： 8307009 DOI： 10.1111/j.1432-1033.1994.tb19956.x

Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956

Keyword Cloud
Cited

28 in total

1. Single amino acid changes in AspRS reveal alternative routes for expanding its tRNA repertoire in vivo.

Authors: Franck Martin; Sharief Barends; Gilbert Eriani
Journal: Nucleic Acids Res Date: 2004-08-02 Impact factor: 16.971

2. Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation.

Authors: A W Curnow; K w Hong; R Yuan; S i Kim; O Martins; W Winkler; T M Henkin; D Söll
Journal: Proc Natl Acad Sci U S A Date: 1997-10-28 Impact factor: 11.205

3. Dynamics of Recognition between tRNA and elongation factor Tu.

Authors: John Eargle; Alexis A Black; Anurag Sethi; Leonardo G Trabuco; Zaida Luthey-Schulten
Journal: J Mol Biol Date: 2008-02-04 Impact factor: 5.469

4. Once there were twenty.

Authors: U L RajBhandary
Journal: Proc Natl Acad Sci U S A Date: 1997-10-28 Impact factor: 11.205

5. The nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori: anticodon-binding domain mutations that impact tRNA specificity and heterologous toxicity.

Authors: Pitak Chuawong; Tamara L Hendrickson
Journal: Biochemistry Date: 2006-07-04 Impact factor: 3.162

Discrimination against misacylated tRNA by chloroplast elongation factor Tu.

1. Single amino acid changes in AspRS reveal alternative routes for expanding its tRNA repertoire in vivo.

2. Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation.

3. Dynamics of Recognition between tRNA and elongation factor Tu.

4. Once there were twenty.

5. The nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori: anticodon-binding domain mutations that impact tRNA specificity and heterologous toxicity.

Review 6. Chloroplast ribosomes and protein synthesis.

Review 7. Translational fidelity and mistranslation in the cellular response to stress.

8. Phenylalanyl-tRNA synthetase editing defects result in efficient mistranslation of phenylalanine codons as tyrosine.

9. Conserved discrimination against misacylated tRNAs by two mesophilic elongation factor Tu orthologs.

10. Thermus thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways.