The molecular dissection of TRIM25's RNA-binding mechanism provides key insights into its antiviral activity.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 39353916.
- Also identified by DOI 10.1038/s41467-024-52918-x and PMC identifier 11445558.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
TRIM25 is an RNA-binding ubiquitin E3 ligase with central but poorly understood roles in the innate immune response to RNA viruses. The link between TRIM25's RNA binding and its role in innate immunity has not been established. Thus, we utilized a multitude of biophysical techniques to identify key RNA-binding residues of TRIM25 and developed an RNA-binding deficient mutant (TRIM25-m9). Using iCLIP2 in virus-infected and uninfected cells, we identified TRIM25's RNA sequence and structure specificity, that it binds specifically to viral RNA, and that the interaction with RNA is critical for its antiviral activity.
Medical subject headings
- Tripartite Motif Proteins
- RNA, Viral
- Ubiquitin-Protein Ligases
- Protein Binding