ArticleThe Journal of biological chemistry2009
Defects in transient tRNA translocation bypass tRNA synthetase quality control mechanisms.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Stress Response and Adaptation Mediated by Amino Acid Misincorporation during Protein Synthesis.Advances in nutrition (Bethesda, Md.) · 2016Review
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Translational fidelity maintenance preventing Ser mis-incorporation at Thr codon in protein from eukaryote.Nucleic acids research · 2013Article
- Coordination of tRNA synthetase active sites for chemical fidelity.The Journal of biological chemistry · 2012Article
- Article
- The balance between pre- and post-transfer editing in tRNA synthetases.FEBS letters · 2010Review
- A glycine hinge for tRNA-dependent translocation of editing substrates to prevent errors by leucyl-tRNA synthetase.FEBS letters · 2009Article
- A paradigm shift for the amino acid editing mechanism of human cytoplasmic leucyl-tRNA synthetase.Biochemistry · 2009Article
- tRNA synthetase: tRNA aminoacylation and beyond.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Quality control mechanisms during protein synthesis are essential to fidelity and cell survival. Leucyl-tRNA synthetase (LeuRS) misactivates non-leucine amino acids including isoleucine, methionine, and norvaline. To prevent translational errors, mischarged tRNA products are translocated 30A from the canonical aminoacylation core to a hydrolytic editing-active site within a completely separate domain. Because it is transient, the tRNA translocation mechanism has been difficult to isolate. We have identified a "translocation peptide" within Escherichia coli LeuRS. Mutations in the translocation peptide cause tRNA to selectively bypass the editing-active site, resulting in mischarging that is lethal to the cell. This bypass mechanism also rescues aminoacylation of an editing site mutation that hydrolyzes correctly charged Leu-tRNA(Leu). Thus, these LeuRS mutants charge tRNA(Leu) but fail to translocate these products to the hydrolytic site, where they are cleared to guard against genetic code ambiguities.
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