Publications by authors named "Qi-Yu Zeng"
Article Synopsis
- * While Tars1 is essential for survival, as evidenced by lethal outcomes in Tars1 knockout mice, deleting Tarsl2 in mice and zebrafish showed no impact on tRNA levels or mRNA translation efficiency.
- * The study found that Tarsl2 mutants experienced severe developmental issues and metabolic changes, indicating that even though Tarsl2 may have some activity, it is not vital for protein synthesis but significantly affects overall development in organisms.
Since numerous RNAs and RBPs prevalently localize to active chromatin regions, many RNA-binding proteins (RBPs) may be potential transcriptional regulators. RBPs are generally thought to regulate transcription via noncoding RNAs. Here, we describe a distinct, dual mechanism of transcriptional regulation by the previously uncharacterized tRNA-modifying enzyme, hTrmt13.
View Article and Find Full Text PDFThe amino acid response (AAR) and unfolded protein response (UPR) pathways converge on eIF2α phosphorylation, which is catalyzed by Gcn2 and Perk, respectively, under different stresses. This close interconnection makes it difficult to specify different functions of AAR and UPR. Here, we generated a zebrafish model in which loss of threonyl-tRNA synthetase (Tars) induces angiogenesis dependent on Tars aminoacylation activity.
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- Aminoacyl-tRNA synthetases (aaRSs) are critical enzymes involved in protein synthesis, and defects in these enzymes can lead to various human diseases.
- Two specific mutations in the human KARS gene, c.1129G>A and c.517T>C, have been linked to hearing impairment, although their precise biochemical effects were previously unclear.
- The study found that while these mutations do not affect the protein's incorporation into a complex in the cytosol, they do lower the levels and alter the structure of cytosolic LysRS, with the c.517T>C mutation showing a complete deficiency in charging mitochondrial tRNA.
Article Synopsis
- N 6-Threonylcarbamoyladenosine (t6A) is a crucial tRNA modification for ensuring accurate protein synthesis in human mitochondria, with key roles played by proteins YrdC and OSGEPL1.
- Mutations in the genes associated with t6A modification, such as those affecting mitochondrial tRNAs and the modifying enzymes, are linked to various human diseases.
- The study revealed that OSGEPL1 is a monomer that utilizes specific tRNA sequences for modification and is influenced by acetylation, providing insights into how tRNA sequence and protein modifications affect t6A levels.
A typical feature of eukaryotic aminoacyl-tRNA synthetases (aaRSs) is the evolutionary gain of domains at either the N- or C-terminus, which frequently mediating protein-protein interaction. TARSL2 (mouse Tarsl2), encoding a threonyl-tRNA synthetase-like protein (ThrRS-L), is a recently identified aaRS-duplicated gene in higher eukaryotes, with canonical functions in vitro, which exhibits a different N-terminal extension (N-extension) from TARS (encoding ThrRS). We found the first half of the N-extension of human ThrRS-L (hThrRS-L) is homologous to that of human arginyl-tRNA synthetase.
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- Human mitochondrial Alanyl-tRNA synthetase (hmtAlaRS) recognizes mitochondrial tRNAAla in a unique way, independent of the typical G3-U70 wobble base pair found in other organisms.
- The study reveals that hmtAlaRS is a monomer and relies on various elements in the acceptor stem for its tRNA recognition.
- Additionally, it identifies the R592W mutation linked to cardiomyopathy and highlights hmtAlaRS's misactivation of Gly and its role in the editing process, providing insights into translational quality control.
Six pathogenic mutations have been reported in human mitochondrial tRNAThr (hmtRNAThr); however, the pathogenic molecular mechanism remains unclear. Previously, we established an activity assay system for human mitochondrial threonyl-tRNA synthetase (hmThrRS). In the present study, we surveyed the structural and enzymatic effects of pathogenic mutations in hmtRNAThr and then focused on m.
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