ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Human aminoacyl-tRNA synthetases as integrators of translation and cell signalling networks.Nature reviews. Molecular cell biology · 2026Review
- Purification and validation of asparaginyl-tRNA synthetase heterodimer with indistinguishable subunits.IUBMB life · 2025Article
- Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1.Nature communications · 2022Article
- Phosphomimetic S207D Lysyl-tRNA Synthetase Binds HIV-1 5'UTR in an Open Conformation and Increases RNA Dynamics.Viruses · 2022Article
- Human lysyl-tRNA synthetase evolves a dynamic structure that can be stabilized by forming complex.Cellular and molecular life sciences : CMLS · 2022Article
- Structural analyses of the malaria parasite aminoacyl-tRNA synthetases provide new avenues for antimalarial drug discovery.Protein science : a publication of the Protein Society · 2021Review
- 3-Dimensional architecture of the human multi-tRNA synthetase complex.Nucleic acids research · 2020Article
- Retractile lysyl-tRNA synthetase-AIMP2 assembly in the human multi-aminoacyl-tRNA synthetase complex.The Journal of biological chemistry · 2019Article
- HIV-1 Exploits a Dynamic Multi-aminoacyl-tRNA Synthetase Complex To Enhance Viral Replication.Journal of virology · 2017Article
- Identification of protein interfaces within the multi-aminoacyl-tRNA synthetase complex: the case of lysyl-tRNA synthetase and the scaffold protein p38.FEBS open bio · 2016Article
- Chemical inhibition of prometastatic lysyl-tRNA synthetase-laminin receptor interaction.Nature chemical biology · 2014Article
- Architecture and metamorphosis.Topics in current chemistry · 2014Review
- Mutations in KARS, encoding lysyl-tRNA synthetase, cause autosomal-recessive nonsyndromic hearing impairment DFNB89.American journal of human genetics · 2013Article
- Rapid screening for potential epitopes reactive with a polycolonal antibody by solution-phase H/D exchange monitored by FT-ICR mass spectrometry.Journal of the American Society for Mass Spectrometry · 2013Article
- Citric acid cycle and the origin of MARS.Trends in biochemical sciences · 2013Article
- Structural switch of lysyl-tRNA synthetase between translation and transcription.Molecular cell · 2013Article
- Dual role for motif 1 residues of human lysyl-tRNA synthetase in dimerization and packaging into HIV-1.The Journal of biological chemistry · 2012Article
- Side chain independent recognition of aminoacyl adenylates by the Hint1 transcription suppressor.The journal of physical chemistry. B · 2012Article
- Uncovering of a short internal peptide activates a tRNA synthetase procytokine.The Journal of biological chemistry · 2012Article
- Unique domain appended to vertebrate tRNA synthetase is essential for vascular development.Nature communications · 2012Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Human lysyl-tRNA synthetase is bound to the multi-tRNA synthetase complex (MSC) that maintains and regulates the aminoacylation and nuclear functions of LysRS. The p38 scaffold protein binds LysRS to the MSC and, only with the appropriate cue, mobilizes LysRS for redirection to the nucleus to interact with the microphthalmia associated transcription factor (MITF). In recent work, an (α(2))(2) LysRS tetramer crystallized to yield a high-resolution structure and raised the question of how LysRS is arranged (dimer or tetramer) in the MSC to interact with p38. To understand the structural organization of the LysRS-p38 complex that regulates LysRS mobilization, we investigated the complex by use of small angle X-ray scattering and hydrogen-deuterium exchange with mass spectrometry in solution. The structure revealed a surprising α(2)β(1):β(1)α(2) organization in which a dimeric p38 scaffold holds two LysRS α(2) dimers in a parallel configuration. Each of the N-terminal 48 residues of p38 binds one LysRS dimer and, in so doing, brings two copies of the LysRS dimer into the MSC. The results suggest that this unique geometry, which reconfigures the LysRS tetramer from α(2):α(2) to α(2)β(1):β(1)α(2), is designed to control both retention and mobilization of LysRS from the MSC.
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