Trim5 α is a sumo substrate

HIGHLIGHTS

• who: Dutrieux et_al Retrovirology ( and collaborators from the (UNIVERSITY) have published the Article: TRIM5 α is a SUMO substrate, in the Journal: (JOURNAL)
• what: The authors show for the first time that TRIM5α SUMOylated both in vitro and in cellulo and that Lysine the main SUMOylation site.
• how: To determine whether TRIM5α itself can be a substrate for SUMO modification the authors employed an in_vitro SUMOylation assay using purified recombinant E1 (SAE1 and SAE2 subunits) and E2 (Ubc9) enzymes recombinant SUMO1 or SUMO2 and increasing doses of GST-tagged PIAS1 E3-ligase or GST . . .
  

   

  

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