Journal Article

PUBDB-2024-07269

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The molecular dissection of TRIM25’s RNA-binding mechanism provides key insights into its antiviral activity

Álvarez, L. ; Haubrich, K. ; Iselin, L. ; Gillioz, L. ; Ruscica, V. ; Lapouge, K. ; Augsten, S. ; Huppertz, I. ; Choudhury, N. R. ; Simon, B. ; Masiewicz, P. ; Lethier, M. ; Cusack, S. ; Rittinger, K. ; Gabel, F. ; Leitner, A. ; Michlewski, G. ; Hentze, M. W. ; Allain, F. H. T. ; Castello, A. (Corresponding author) ; Hennig, J. (Corresponding author)

2024
Nature Publishing Group UK [London]

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Please use a persistent id in citations: doi:10.1038/s41467-024-52918-x  doi:10.3204/PUBDB-2024-07269

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.

Note: (DFG) via grants HE7291/1-1 and HE7291/8-1

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Contributing Institute(s):

1. EMBL-User (EMBL-User)
2. EMBL (EMBL)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P12 (PETRA III)

Appears in the scientific report 2024

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