ArticleNucleic acids research2025
Unexpected enzymatic function of an ancient nucleic acid-binding fold.
Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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
1 citing paper in PubMed.
- Human aminoacyl-tRNA synthetases as integrators of translation and cell signalling networks.Nature reviews. Molecular cell biology · 2026Review
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Aminoacyl-tRNA synthetases (ARSs) are indispensable for all living organisms and their associated aminoacyl-tRNA editing domains ensure the fidelity of translation. In eukaryotes, ARSs form a multi-aminoacyl-tRNA synthetase complex (MSC), which is assembled together with several nonsynthetase scaffolding proteins. The MSC found in Trypanosoma brucei (Tb) includes two proteins with oligosaccharide/oligonucleotide-binding (OB) folds-MSC-associated protein 1 (MCP1) and MCP2-and one known trans-editing factor, MCP3, an Ala-tRNA deacylase. The activity of MCP1 was unexplored until now. Our study shows that recombinantly-expressed and purified MCP1 also deacylates Ala-tRNAs despite lacking known tRNA-editing domain homology. Domain deletion studies reveal that the OB-fold houses the catalytic pocket and mutation of any one of three conserved OB-fold residues (K326, R331, S335) abolishes activity. Assays with Saccharomyces cerevisiae Arc1p reveal that MCP1's deacylation activity is conserved across organisms. This discovery explains the 3' CCA-end binding activity of this protein family and uncovers an ancient nucleic acid binding domain's unexpected enzymatic function.
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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 Socratic graph.