tRNAs play a central role in protein translation, acting as the carrier of amino acids. By cloning microRNAs, we unexpectedly obtained some tRNA fragments generated by tRNA cleavage in the anticodon loop. These tRNA fragments are present in many cell lines and different mouse tissues. In addition, various stress conditions can induce this tRNA cleavage event in mammalian cells. More importantly, angiogenin (ANG), a member of RNase A superfamily, appears to be the nuclease which cleaves tRNAs into tRNA halves in vitro and in vivo. These results imply that angiogenin plays an important physiological role in cell stress response, except for the known function of inducing angiogenesis.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.febslet.2008.12.043 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Role of tRNA-Derived Fragments in Protozoan Parasite Biology.
Cells
January 2025
Division of Infectious Diseases, School of Medicine, Stanford University, Stanford, CA 94305, USA.
tRNA molecules are among the most fundamental and evolutionarily conserved RNA types, primarily facilitating the translation of genetic information from mRNA into proteins. Beyond their canonical role as adaptor molecules during protein synthesis, tRNAs have evolved to perform additional functions. One such non-canonical role for tRNAs is through the generation of tRNA-derived fragments via specific cleavage processes.
View Article and Find Full Text PDFRNase P cleavage of pseudoknot substrates reveals differences in active site architecture that depend on residue N-1 in the 5' leader.
RNA Biol
December 2025
Department of Cell and Molecular Biology, Biomedical Centre, Uppsala University, Uppsala, Sweden.
We show that a small biotin-binding RNA aptamer that folds into a pseudoknot structure acts as a substrate for bacterial RNase P RNA (RPR) with and without the RNase P C5 protein. Cleavage in the single-stranded region in loop 1 was shown to depend on the presence of a RCCA-motif at the 3' end of the substrate. The nucleobase and the 2'hydroxyl at the position immediately 5' of the cleavage site contribute to both cleavage efficiency and site selection, where C at this position induces significant cleavage at an alternative site, one base upstream of the main cleavage site.
View Article and Find Full Text PDFSLFN11-mediated tRNA regulation induces cell death by disrupting proteostasis in response to DNA-damaging agents.
bioRxiv
January 2025
Institute for Advanced Biosciences, Keio University, Tsuruoka, 997-0017, Japan.
DNA-damaging agents (DDAs) have long been used in cancer therapy. However, the precise mechanisms by which DDAs induce cell death are not fully understood and drug resistance remains a major clinical challenge. Schlafen 11 (SLFN11) was identified as the gene most strongly correlated with the sensitivity to DDAs based on mRNA expression levels.
View Article and Find Full Text PDFSchlesneria sphaerica sp. nov., a neutrophilic, xylan-degrading planctomycete from a mountain wetland, and emended description of the genus Schlesneria.
FEMS Microbiol Lett
January 2025
Winogradsky Institute of Microbiology, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow 119071, Russia.
Aerobic chemoorganotrophic planctomycetes of the genus Schlesneria colonize a wide spectrum of freshwater ecosystems. The only described species of this genus, S. paludicola, is represented by ellipsoid-shaped, moderately acidophilic bacteria isolated from acidic peat bogs.
View Article and Find Full Text PDFRecognition and cleavage of human tRNA methyltransferase TRMT1 by the SARS-CoV-2 main protease.
Elife
January 2025
Department of Chemistry & Biochemistry, University of Delaware, Newark, United States.
The SARS-CoV-2 main protease (M or Nsp5) is critical for production of viral proteins during infection and, like many viral proteases, also targets host proteins to subvert their cellular functions. Here, we show that the human tRNA methyltransferase TRMT1 is recognized and cleaved by SARS-CoV-2 M. TRMT1 installs the ,-dimethylguanosine (m2,2G) modification on mammalian tRNAs, which promotes cellular protein synthesis and redox homeostasis.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!