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Cytoplasmically localized tRNA-derived fragments inhibit translation in S2 cells. | LitMetric

Cytoplasmically localized tRNA-derived fragments inhibit translation in S2 cells.

Turk J Biol

Department of Molecular Biology and Genetics, İzmir Institute of Technology, İzmir, Turkey.

Published: January 2022

AI Article Synopsis

  • tRNAs not only carry amino acids for protein synthesis but also produce short fragments (tRFs) that may help regulate gene expression.
  • Despite advancements in understanding tRFs, their specific locations, interactions with proteins, and mechanisms of action in translation regulation are still unclear.
  • In experiments with S2 cells, synthetic tRFs were found in distinct cytoplasmic locations near GW182 and XRN1 proteins, and while they slightly reduced cell proliferation, they inhibited translation without significantly affecting the overall polysome profile.

Article Abstract

Transfer ribonucleic acids (tRNAs) serve not only as amino acid carriers during translation but also as a template for the biogenesis of short fragments that can regulate gene expression. Despite recent progress in the function of tRNA-derived fragments (tRFs), their intracellular localization, protein partners, and role in regulating translation are not well understood. We used synthetic tRFs to investigate their localization and function in S2 cells. Under our experimental setting, all synthetic tRFs tested were localized at distinct sites within the cytoplasm in a similar manner in S2 cells. Cytoplasmically-localized tRFs were positioned in close proximity to GW182 and XRN1 proteins. Functionally, tRFs, which slightly suppressed proliferation in S2 cells, inhibited translation without any major shift in the polysome profile. These results suggest that 5'-tRFs are cytoplasmically-localized and regulate gene expression through inhibition of translation in .

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10387997PMC
http://dx.doi.org/10.55730/1300-0152.2610DOI Listing

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