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Details on Person In addition to sensing non-self 5′-ppp-RNA, IFN-induced prot...
| Class:Id | Summation:9690759 |
|---|---|
| _displayName | In addition to sensing non-self 5′-ppp-RNA, IFN-induced prot... |
| _timestamp | 2025-10-13 15:55:50 |
| created | [InstanceEdit:9690755] Shamovsky, Veronica, 2020-06-05 |
| literatureReference | [LiteratureReference:9684546] Inhibition of translation by IFIT family members is determined by their ability to interact selectively with the 5'-terminal regions of cap0-, cap1- and 5'ppp- mRNAs [LiteratureReference:9690752] tRNA binding, structure, and localization of the human interferon-induced protein IFIT5 [LiteratureReference:9690762] Broad and adaptable RNA structure recognition by the human interferon-induced tetratricopeptide repeat protein IFIT5 |
| modified | [InstanceEdit:9692472] Shamovsky, Veronica, 2020-06-24 [InstanceEdit:9714093] Shamovsky, Veronica, 2021-02-02 [InstanceEdit:9968348] Shamovsky, Veronica, 2025-10-13 |
| text | In addition to sensing non-self 5′-ppp-RNA, IFN-induced protein with tetratricopeptide repeats (TPR) 5 (IFIT5) binds a range of endogenous human RNAs with 5′ mono- or triphosphate ends, with binding preferences and specificities described in detail by Katibah et al. (2014). These include RNAs, such as precursor and processed tRNAs, poly-U-tailed tRNA fragments, and Alu-related small NF90-associated RNA (snaR) transcripts (Katibah GE et al., 2013; 2014; Kumar P et al., 2014). This Reactome event describes IFIT5 recognition of tRNA. Electrophoretic mobility shift assays (EMSA) with radiolabeled RNAs demonstrated that recombinant IFIT5 binds cellular 3′-truncated tRNA with higher affinity than the 5′-p and 5′-ppp ends of West Nile virus (WNV) RNA fragments (first 30 nucleotides) (Katibah GE et al., 2014). IFIT5 also preferentially associates with 3′-truncated initiator methionine (iMet) tRNA fragments compared to the full-length iMet tRNA or its anticodon stem-loop (Katibah GE et al., 2013). Structural and mutagenesis studies revealed distinct binding modes for immature ppp-tRNA and mature p-tRNA. Unprocessed ppp-tRNA is thought to occupy the central RNA-binding channel, whereas mature p-tRNA interacts with a separate binding cleft on the lower surface of IFIT5, outside the central cavity (Katibah GE et al., 2013; 2014). Similarly to IFIT5, IFIT1 also displays tRNA-binding activity (Kumar P et al., 2014). |
| (summation) | [Reaction:9690683] IFIT5 binds tRNA [Homo sapiens] |
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No pathways have been reviewed or authored by In addition to sensing non-self 5′-ppp-RNA, IFN-induced prot... (9690759)
