Structural highlights
FunctionPublication Abstract from PubMedTranslational regulation by non-coding RNAs is a mechanism commonly used by cells to fine-tune gene expression. A fragment derived from an archaeal valine tRNA (Val-tRF) has been previously identified to bind the small subunit of the ribosome and inhibit translation in Haloferax volcanii Here, we present three cryo-electron microscopy structures of Val-tRF bound to the small subunit of Sulfolobus acidocaldarius ribosomes at resolutions between 4.02 and 4.53 A. Within these complexes, Val-tRF was observed to bind to conserved RNA-interacting sites, including the ribosomal decoding center. The binding of Val-tRF destabilizes helices h24, h44, and h45 and the anti-Shine-Dalgarno sequence of 16S rRNA. The binding position of this molecule partially overlaps with the translation initiation factor aIF1A and occludes the mRNA P-site codon. Moreover, we found that the binding of Val-tRF is associated with steric hindrance of the H69 base of 23S rRNA in the large ribosome subunit, thereby preventing 70S assembly. Our data exemplify how tRNA-derived fragments bind to ribosomes and provide new insights into the mechanisms underlying translation inhibition by Val-tRFs. Structural basis of translation inhibition by a valine tRNA-derived fragment.,Wu Y, Ni MT, Wang YH, Wang C, Hou H, Zhang X, Zhou J Life Sci Alliance. 2024 Apr 10;7(6):e202302488. doi: 10.26508/lsa.202302488. , Print 2024 Jun. PMID:38599770[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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