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Related Experiment Video

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In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
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TRIM5α is a SUMO substrate.

Jacques Dutrieux1, Débora M Portilho2, Nathalie J Arhel3

  • 1INSERM UMR-S 1124, Université Paris Descartes, 45 rue des Saints-Pères, 75006, Paris, France. jacques.dutrieux@inserm.fr.

Retrovirology
|April 17, 2015
PubMed
Summary

The SUMOylation machinery is crucial for TRIM5α antiviral activity against retroviruses. TRIM5α is SUMOylated, but direct modification is not essential for its restriction function.

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Area of Science:

  • Virology
  • Molecular Biology
  • Cellular Biology

Background:

  • TRIM5α restricts retroviral infections by inhibiting viral replication.
  • SUMOylation machinery and SUMO interacting motifs (SIMs) are implicated in TRIM5α regulation.
  • Previous studies showed SIM mutations abolish TRIM5α activity, but SUMOylation site mutations did not affect its function.

Purpose of the Study:

  • To investigate the role of SUMOylation in TRIM5α antiviral activity.
  • To determine if TRIM5α is a direct substrate of SUMOylation.
  • To identify the specific SUMOylation site on TRIM5α.

Main Methods:

  • Overexpression and knockdown of SUMO1 and Ubc9.
  • In vitro and in cellulo SUMOylation assays.
  • Site-directed mutagenesis of TRIM5α SUMOylation site (Lysine 10).

Main Results:

  • SUMO1 overexpression enhanced TRIM5α restriction; SUMO1 or Ubc9 knockdown inhibited it.
  • TRIM5α was confirmed to be SUMOylated in vitro and in cellulo.
  • Lysine 10 was identified as the primary SUMOylation site, but its mutation did not abolish antiviral activity.

Conclusions:

  • SUMOylation machinery is essential for TRIM5α-mediated retroviral restriction.
  • TRIM5α is a substrate for SUMO 1 and SUMO 2.
  • Non-covalent interactions with SUMO or SUMOylated proteins, rather than direct TRIM5α SUMOylation, are critical for its antiviral function.