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-Structure paper
| タイトル | Structural basis of translation inhibition by a valine tRNA-derived fragment. |
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| ジャーナル・号・ページ | Life Sci Alliance, Vol. 7, Issue 6, Year 2024 |
| 掲載日 | 2024年4月10日 |
著者 | Yun Wu / Meng-Ting Ni / Ying-Hui Wang / Chen Wang / Hai Hou / Xing Zhang / Jie Zhou / ![]() |
| PubMed 要旨 | Translational 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 ...Translational 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 Here, we present three cryo-electron microscopy structures of Val-tRF bound to the small subunit of ribosomes at resolutions between 4.02 and 4.53 Å. 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. |
リンク | Life Sci Alliance / PubMed:38599770 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 4.1 - 4.62 Å |
| 構造データ | EMDB-37604, PDB-8wkp: EMDB-37733, PDB-8wq2: EMDB-37734, PDB-8wq4: |
| 化合物 | ![]()
ChemComp-UNL: |
| 由来 |
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キーワード | RIBOSOME / Sulfolobus acidocaldarius ribosome |
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sulfolobus acidocaldarius dsm 639 (好気性・好酸性)
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