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The molecular dissection of TRIM25's RNA-binding mechanism provides key insights into its antiviral activity

Title data

Álvarez, Lucía ; Haubrich, Kevin ; Iselin, Louisa ; Gillioz, Laurent ; Ruscica, Vincenzo ; Lapouge, Karine ; Augsten, Sandra ; Huppertz, Ina ; Choudhury, Nila-Roy ; Simon, Bernd ; Masiewicz, Pawel ; Lethier, Mathilde ; Cusack, Stephen ; Rittinger, Katrin ; Gabel, Frank ; Leitner, Alexander ; Michlewski, Gracjan ; Hentze, Matthias ; Allain, Frédéric H. T. ; Castello, Alfredo ; Hennig, Janosch:
The molecular dissection of TRIM25's RNA-binding mechanism provides key insights into its antiviral activity.
In: Nature Communications. Vol. 15 (2024) Issue 1 . - 8485.
ISSN 2041-1723
DOI: https://doi.org/10.1038/s41467-024-52918-x

Official URL: Volltext

Project information

Project financing: Deutsche Forschungsgemeinschaft

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry IV - Biophysical Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry IV - Biophysical Chemistry > Chair Biochemistry IV - Biophysical Chemistry - Univ.-Prof. Dr. Janosch Hennig
Research Institutions > Central research institutes > Nordbayerisches Zentrum für NMR-Spektroskopie - NMR-Zentrum
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 500 Natural sciences
500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 07 Oct 2024 07:35
Last Modified: 07 Oct 2024 07:35
URI: https://eref.uni-bayreuth.de/id/eprint/90561