ArticleStructure (London, England : 1993)2012
Internally deleted human tRNA synthetase suggests evolutionary pressure for repurposing.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 36 citations in OpenAlex.
- Relationship between Jo-1 B Cell Epitope Profile and Clinical Features of Anti-Synthetase Syndrome.ACR open rheumatology · 2024Article
- Clinical and prognostic associations of anti-Jo-1 antibody levels in patients with antisynthetase syndrome.Respiratory research · 2024Article
- Towards a Cure for HARS Disease.Genes · 2023Review
- Longitudinal assessment of reactivity and affinity profile of anti-Jo1 autoantibodies to distinct HisRS domains and a splice variant in a cohort of patients with myositis and anti-synthetase syndrome.Arthritis research & therapy · 2022Article
- Serum-circulating His-tRNA synthetase inhibits organ-targeted immune responses.Cellular & molecular immunology · 2021Article
- Tryptophanyl-tRNA Synthetase as a Potential Therapeutic Target.International journal of molecular sciences · 2021Review
- CMT disease severity correlates with mutation-induced open conformation of histidyl-tRNA synthetase, not aminoacylation loss, in patient cells.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Aminoacyl-tRNA synthetases as therapeutic targets.Nature reviews. Drug discovery · 2019Review
- Structural control of caspase-generated glutamyl-tRNA synthetase by appended noncatalytic WHEP domains.The Journal of biological chemistry · 2018Article
- The Usher Syndrome Type IIIB Histidyl-tRNA Synthetase Mutation Confers Temperature Sensitivity.Biochemistry · 2017Article
- Alternative splicing creates two new architectures for human tyrosyl-tRNA synthetase.Nucleic acids research · 2016Article
- Structural basis for recognition of G-1-containing tRNA by histidyl-tRNA synthetase.Nucleic acids research · 2015Article
- Comparison of histidine recognition in human and trypanosomatid histidyl-tRNA synthetases.Biochimie · 2014Article
- Human tRNA synthetase catalytic nulls with diverse functions.Science (New York, N.Y.) · 2014Article
- Secreted histidyl-tRNA synthetase splice variants elaborate major epitopes for autoantibodies in inflammatory myositis.The Journal of biological chemistry · 2014Article
- Article
- Emergence and evolution.Topics in current chemistry · 2014Review
- Transfer RNA and human disease.Frontiers in genetics · 2014Review
- Architecture and metamorphosis.Topics in current chemistry · 2014Review
- Regulated capture by exosomes of mRNAs for cytoplasmic tRNA synthetases.The Journal of biological chemistry · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 2 institutions in 2 countries.
Funding
Abstract
Aminoacyl-tRNA synthetases (AARSs) catalyze aminoacylation of tRNAs in the cytoplasm. Surprisingly, AARSs also have critical extracellular and nuclear functions. Evolutionary pressure for new functions might be manifested by splice variants that skip only an internal catalytic domain (CD) and link noncatalytic N- and C-terminal polypeptides. Using disease-associated histidyl-tRNA synthetase (HisRS) as an example, we found an expressed 171-amino acid protein (HisRSΔCD) that deleted the entire CD, and joined an N-terminal WHEP to the C-terminal anticodon-binding domain (ABD). X-ray crystallography and three-dimensional NMR revealed the structures of human HisRS and HisRSΔCD. In contrast to homodimeric HisRS, HisRSΔCD is monomeric, where rupture of the ABD's packing with CD resulted in a dumbbell-like structure of flexibly linked WHEP and ABD domains. In addition, the ABD of HisRSΔCD presents a distinct local conformation. This natural internally deleted HisRS suggests evolutionary pressure to reshape AARS tertiary and quaternary structures for repurposing.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.