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TRIM25 Binds RNA to Modulate Cellular Anti-viral Defense
Jacint G Sanchez1, Konstantin M J Sparrer2, Cindy Chiang2
1Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA.
Journal of Molecular Biology
|October 21, 2018
Summary
Tripartite motif 25 (TRIM25) binds RNA, modulating its own activity and cellular localization. This RNA interaction is crucial for TRIM25
Area of Science:
- Molecular Biology
- Immunology
- Virology
Background:
- TRIM25 is a RING-type E3 ubiquitin ligase involved in RNA-dependent processes and innate immunity.
- TRIM25 acts as an effector for RIG-I and ZAP, key sensors of viral RNA.
- The RNA-binding capacity of TRIM25 and its functional relevance remain largely uncharacterized.
Purpose of the Study:
- To investigate the RNA-binding properties of TRIM25.
- To elucidate the functional consequences of TRIM25-RNA interactions in antiviral defense.
Main Methods:
- Biochemical characterization of TRIM25's RNA-binding activity.
- In vitro assays to assess ubiquitination activity and cellular localization.
- Analysis of TRIM25 structure and function in response to viral RNA.
Main Results:
- TRIM25 binds both single-stranded and double-stranded RNA.
- The SPRY domain and a lysine-rich motif are critical for RNA binding.
- RNA binding enhances TRIM25 ubiquitination activity, alters its cellular localization, and impacts its antiviral function.
Conclusions:
- RNA binding is a key regulatory mechanism for TRIM25 activity and function.
- TRIM25-RNA interactions influence ubiquitination, protein structure, and subcellular localization during viral infections.
- Understanding TRIM25's RNA-binding is vital for elucidating innate antiviral immune responses.
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