ArticleBiochemistry2009
A paradigm shift for the amino acid editing mechanism of human cytoplasmic leucyl-tRNA synthetase.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Simultaneous determination of cytosolic aminoacyl-tRNA synthetase activities by LC-MS/MS.Nucleic acids research · 2024Article
- Exercise May Promote Skeletal Muscle Hypertrophy via Enhancing Leucine-Sensing: Preliminary Evidence.Frontiers in physiology · 2021Article
- Aminoacyl-tRNA synthetases as therapeutic targets.Nature reviews. Drug discovery · 2019Review
- Coordination of the leucine-sensing Rag GTPase cycle by leucyl-tRNA synthetase in the mTORC1 signaling pathway.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Loss of function mutations in VARS encoding cytoplasmic valyl-tRNA synthetase cause microcephaly, seizures, and progressive cerebral atrophy.Human genetics · 2018Article
- [Clinical feature and molecular diagnostic analysis of the first non-caucasian child with infantile liver failure syndrome type 1].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2017Article
- Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase.Nucleic acids research · 2011Article
- tRNA synthetase: tRNA aminoacylation and beyond.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Leucyl-tRNA synthetase (LeuRS) has been identified as a target for a novel class of boron-containing small molecules that bind to its editing active site. When the 3' end of tRNA(Leu) binds to the editing active site, the boron cross-links to the cis-diols of its terminal ribose. The cross-linked RNA-protein complex blocks the overall aminoacylation activity of the enzyme. Similar to those of other LeuRSs, the human cytoplasmic enzyme (hscLeuRS) editing active site resides in a discrete domain called the connective polypeptide 1 domain (CP1), where mischarged tRNA binds for hydrolysis of the noncognate amino acid. The editing site of hscLeuRS includes a highly conserved threonine discriminator and universally conserved aspartic acid that were mutationally characterized. Substitution of the threonine residue to alanine uncoupled specificity as in other LeuRSs. However, the introduction of bulky residues into the amino acid binding pocket failed to block deacylation of tRNA, indicating that the architecture of the amino acid binding pocket is different compared to that of other characterized LeuRSs. In addition, mutation of the universally conserved aspartic acid abolished tRNA(Leu) deacylation. Surprisingly though, this editing-defective hscLeuRS maintained fidelity. It is possible that an alternate editing mechanism may have been activated upon failure of the post-transfer editing active site.
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